Untangling the adaptive strategies of thermophilic bacterium Anoxybacillus rupiensis TPH1 under low temperature.


Journal

Extremophiles : life under extreme conditions
ISSN: 1433-4909
Titre abrégé: Extremophiles
Pays: Germany
ID NLM: 9706854

Informations de publication

Date de publication:
17 Jul 2024
Historique:
received: 28 12 2023
accepted: 10 06 2024
medline: 18 7 2024
pubmed: 18 7 2024
entrez: 17 7 2024
Statut: epublish

Résumé

The present study investigates the low temperature tolerance strategies of thermophilic bacterium Anoxybacillus rupiensis TPH1, which grows optimally at 55 °C , by subjecting it to a temperature down-shift of 10 °C (45 °C) for 4 and 6 h followed by studying its growth, morphophysiological, molecular and proteomic responses. Results suggested that although TPH1 experienced increased growth inhibition, ROS production, protein oxidation and membrane disruption after 4 h of incubation at 45 °C yet maintained its DNA integrity and cellular structure through the increased expression of DNA damage repair and cell envelop synthesizing proteins and also progressively alleviated growth inhibition by 20% within two hours i.e., 6 h, by inducing the expression of antioxidative enzymes, production of unsaturated fatty acids, capsular and released exopolysaccharides and forming biofilm along with chemotaxis proteins. Conclusively, the adaptation of Anoxybacillus rupiensis TPH1 to lower temperature is mainly mediated by the synthesis of large numbers of defense proteins and exopolysaccharide rich biofilm formation.

Identifiants

pubmed: 39020126
doi: 10.1007/s00792-024-01346-2
pii: 10.1007/s00792-024-01346-2
doi:

Substances chimiques

Bacterial Proteins 0

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

31

Subventions

Organisme : Institute of Eminence, Banaras Hindu University, Varanasi, India.
ID : IoE-6031

Informations de copyright

© 2024. The Author(s), under exclusive licence to Springer Nature Japan KK.

Références

Abee T, Kovács AT, Kuipers OP, van der Veen S (2011) Biofilm formation and dispersal in Gram-positive bacteria. Curr Opin Biotechnol 22:172–179. https://doi.org/10.1016/j.copbio.2010.10.016
doi: 10.1016/j.copbio.2010.10.016 pubmed: 21109420
Aebi H (1984) Catalase in-vitro. Methods Enzymol 5:121–126. https://doi.org/10.1016/S0076-68798405016-3
doi: 10.1016/S0076-68798405016-3
Alcorlo M, Straume D, Lutkenhaus J, Håvarstein LS, Hermoso JA (2020) Structural characterization of the essential cell division protein FtsE and its interaction with FtsX in Streptococcus pneumoniae. Mbio 11:10–1128. https://doi.org/10.1128/mBio.01488-20
doi: 10.1128/mBio.01488-20
Amend JP, Shock EL (2001) Energetics of overall metabolic reactions of thermophilic and hyperthermophilic Archaea and Bacteria. FEMS Microbiol Rev 25:175–243. https://doi.org/10.1111/j.1574-6976.2001.tb00576.x
doi: 10.1111/j.1574-6976.2001.tb00576.x pubmed: 11250035
Angelin J, Kavitha M (2020) Exopolysaccharides from probiotic bacteria and their health potential. Int J Biol Macromol 162:853–865. https://doi.org/10.1016/j.ijbiomac.2020.06.190
doi: 10.1016/j.ijbiomac.2020.06.190 pubmed: 32585269 pmcid: 7308007
Bates LS, Waldren RP, Tear ID (1975) Rapid determination of free proline for water stress studies. Plant Soil 39:205–207. https://doi.org/10.1007/BF00018060
doi: 10.1007/BF00018060
Becskei A, Rahaman S (2022) The life and death of RNA across temperatures. Comput Struct Biotechnol 20:4325–4336. https://doi.org/10.1016/j.csbj.2022.08.008
doi: 10.1016/j.csbj.2022.08.008
Bendia AG, Araujo GG, Pulschen AA, Contro B, Duarte RT, Rodrigues F, Galante D, Pellizari VH (2018) Surviving in hot and cold: psychrophiles and thermophiles from Deception Island volcano, Antarctica. Extremophiles 22:917–929. https://doi.org/10.1007/s00792-018-1048-1
doi: 10.1007/s00792-018-1048-1 pubmed: 30109444
Bernard R, Marquis KA, Rudner DZ (2010) Nucleoid occlusion prevents cell division during replication fork arrest in Bacillus subtilis. Mol Microbiol 78:866–882. https://doi.org/10.1111/j.1365-2958.2010.07369.x
doi: 10.1111/j.1365-2958.2010.07369.x pubmed: 20807205 pmcid: 2978284
Bhattacharjee S, Srivastava A, Parida A, Gupta N, Singh P, Singh SS, Mishra AK (2023) Efficient biodegradation of sodium dodecyl sulfate SDS by the cyanobacterium Fischerella sp. lmga1 harbouring SdsA1 hydrolase. J Appl Phycol 15:1–13. https://doi.org/10.1007/s10811-023-02961-w
doi: 10.1007/s10811-023-02961-w
Blaby IK, Lyons BJ, Wroclawska-Hughes E, Phillips GC, Pyle TP, Chamberlin SG, Benner SA, Lyons TJ, de Crécy-Lagard V, de Crécy E (2012) Experimental evolution of a facultative thermophile from a mesophilic ancestor. Appl Environ Microbiol 78:144–155. https://doi.org/10.1128/AEM.05773-11
doi: 10.1128/AEM.05773-11 pubmed: 22020511 pmcid: 3255606
Bloom LB (2009) Loading clamps for DNA replication and repair. DNA Repair Amst 8:570–578. https://doi.org/10.1016/j.dnarep.2008.12.014
doi: 10.1016/j.dnarep.2008.12.014 pubmed: 19213612 pmcid: 2691718
Boecker S, Slaviero G, Schramm T, Szymanski W, Steuer R, Link H, Klamt S (2021) Deciphering the physiological response of Escherichia coli under high ATP demand. Mol Syst Biol 17:e10504. https://doi.org/10.15252/msb.202110504
Borisov VB, Siletsky SA, Paiardini A, Hoogewijs D, Forte E, Giuffre A, Poole RK (2021) Bacterial oxidases of the cytochrome bd family: Redox enzymes of unique structure, function, and utility as drug targets. Antioxid Redox Signal 34:1280–1318. https://doi.org/10.1089/ars.2020.8039
doi: 10.1089/ars.2020.8039 pubmed: 32924537 pmcid: 8112716
Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248–254. https://doi.org/10.1006/abio.1976.9999
doi: 10.1006/abio.1976.9999 pubmed: 942051
Broschat KO, Gorka C, Page JD, Martin-Berger CL, Davies MS, Huang Hc HC, Gulve EA, Salsgiver WJ, Kasten TP (2002) Kinetic characterization of human glutamine-fructose-6-phosphate amidotransferase I: potent feedback inhibition by glucosamine 6-phosphate. J Biol Chem 277:14764–14770. https://doi.org/10.1074/jbc.M201056200.v
doi: 10.1074/jbc.M201056200.v pubmed: 11842094
Bulat SA, Alekhina IA, Blot M, Petit JR, De Angelis M, Wagenbach D, Lipenkov VY, Vasilyeva LP, Wloch DM, Raynaud D, Lukin VV (2004) DNA signature of thermophilic bacteria from the aged accretion ice of Lake Vostok, Antarctica: Implications for searching for life in extreme icy environments. Int J Astrobiol 3:1–12. https://doi.org/10.1017/S1473550404001879
doi: 10.1017/S1473550404001879
Burby PE, Simmons LA (2020) Regulation of cell division in bacteria by monitoring genome integrity and DNA replication status. J Bacteriol 202:10–1128. https://doi.org/10.1128/jb.00408-19
doi: 10.1128/jb.00408-19
Butala M, Žgur-Bertok D, Busby SJ (2009) The bacterial LexA transcriptional repressor. Cell Mol Life Sci 66:82–93. https://doi.org/10.1007/s00018-008-8378-6
doi: 10.1007/s00018-008-8378-6 pubmed: 18726173
Carusillo A, Mussolino C (2020) DNA damage: from threat to treatment. Cells 9:1665. https://doi.org/10.3390/cells9071665
doi: 10.3390/cells9071665 pubmed: 32664329 pmcid: 7408370
Chakraborty S, Mishra AK (2021) Effects of zinc toxicity on the nitrogen-fixing cyanobacterium Anabaena sphaerica-ultastructural, physiological and biochemical analyses. Environ Sci Pollut Res 28:33292–33306. https://doi.org/10.1007/s11356-021-12882-1
doi: 10.1007/s11356-021-12882-1
Chandra S, Khan S, Avula B, Lata H, Yang MH, Elsohly MA, Khan IA (2014) Assessment of total phenolic and flavonoid content, antioxidant properties, and yield of aeroponically and conventionally grown leafy vegetables and fruit crops: A comparative study. Evidence-Based Complement Altern Med. https://doi.org/10.1155/2014/253875
doi: 10.1155/2014/253875
Chatterjee N, Walker GC (2017) Mechanisms of DNA damage, repair, and mutagenesis. Environ Mol Mutagen 58:235–263. https://doi.org/10.1002/em.22087
doi: 10.1002/em.22087 pubmed: 28485537 pmcid: 5474181
Choudhury R, Srivastava S (2001) Zinc resistance mechanisms in bacteria. Curr Sci 81:768–775. http://www.jstor.org/stable/24106396
Colombo G, Clerici M, Garavaglia ME, Giustarini D, Rossi R, Milzani A, Dalle-Donne I (2016) A step-by-step protocol for assaying protein carbonylation in biological samples. J Chromatogr B Anal Technol Biomed Life Sci 1019:178–190. https://doi.org/10.1016/j.jchromb.2015.11.052
doi: 10.1016/j.jchromb.2015.11.052
de Kok A, Hengeveld AF, Martin A, Westphal AH (1998) The pyruvate dehydrogenase multi-enzyme complex from Gram-negative bacteria. Biochim Biophys Acta Protein Struct Mol Enzymol 1385:353–366. https://doi.org/10.1016/S0167-4838(98)00079-X
doi: 10.1016/S0167-4838(98)00079-X
Dionisio-Sese ML, Tobita S (1998) Antioxidant responses of rice seedlings to salinity stress. Plant Sci 135:1–9. https://doi.org/10.1016/S0168-94529800025-9
doi: 10.1016/S0168-94529800025-9
Dubois M, Gilles KA, Hamilton JK, Rebers PA, Smith F (1956) Colorimetric method for determination of sugars and related substances. Anal Chem 28:350–356. https://doi.org/10.1021/ac60111a017
doi: 10.1021/ac60111a017
Dumont S, Rivoal J (2019) Consequences of oxidative stress on plant glycolytic and respiratory metabolism. Front Plant Sci 10:166. https://doi.org/10.3389/fpls.2019.00166
doi: 10.3389/fpls.2019.00166 pubmed: 30833954 pmcid: 6387960
El Razak AA, Ward AC, Glassey J (2014) Screening of marine bacterial producers of polyunsaturated fatty acids and optimisation of production. Microb Ecol 67:454–464. https://doi.org/10.1007/s00248-013-0332-y
doi: 10.1007/s00248-013-0332-y pubmed: 24292901
Farmer J (1998) Thermophiles, early biosphere evolution, and the origin of life on Earth: implications for the exobiological exploration of Mars. J Geophys Res Planets 103:28457–28461. https://doi.org/10.1029/98JE01542
doi: 10.1029/98JE01542
Fasnacht M, Polacek N (2021) Oxidative stress in bacteria and the central dogma of molecular biology. Front Mol Biosci 8:1–13. https://doi.org/10.3389/fmolb.2021.671037
doi: 10.3389/fmolb.2021.671037
Fields ML, Lee PC, Wang D (1974) Relationship of soil constituents to spore counts and heat resistance of Bacillus stearothermophilus. Can J Microbiol 20:1625–1631. https://doi.org/10.1139/m74-253
doi: 10.1139/m74-253 pubmed: 4441977
Figueiredo J, Henriques MX, Catalão MJ, Pinheiro S, Narciso AR, Mesquita F, Saraiva BM, Carido M, Cabanes D, Pinho MG, Filipe SR (2022) Encapsulation of the septal cell wall protects Streptococcus pneumoniae from its major peptidoglycan hydrolase and host defenses. PLoS Pathog 18:e1010516. https://doi.org/10.1371/journal.ppat.1010516
doi: 10.1371/journal.ppat.1010516 pubmed: 35731836 pmcid: 9216600
Fincan SA, Enez B, Bekler ÖS, FM, (2014) Purification and characterization of thermostable α-amylase from thermophilic Anoxybacillus flavithermus. Carbohydr Polym 102:144–150. https://doi.org/10.1016/j.carbpol.2013.10.048
doi: 10.1016/j.carbpol.2013.10.048
Fong JNC, Yildiz FH (2015) Biofilm matrix proteins. Microbiol Spectr. https://doi.org/10.1128/microbiolspec.MB-0004-2014
doi: 10.1128/microbiolspec.MB-0004-2014 pubmed: 26104709
Fujita Y, Matsuoka H, Hirooka K (2007) Regulation of fatty acid metabolism in bacteria. Mol Microbiol 66:829–839. https://doi.org/10.1111/j.1365-2958.2007.05947.x
doi: 10.1111/j.1365-2958.2007.05947.x pubmed: 17919287
Gai C, Liu Z, Han G, Peng N, Fan A (2015) Combustion behavior and kinetics of low-lipid microalgae via thermogravimetric analysis. Bioresour Technol 181:148–154. https://doi.org/10.1016/j.biortech.2015.01.045
doi: 10.1016/j.biortech.2015.01.045 pubmed: 25647025
Gaitonde MK (1967) A spectrophotometric method for the direct determination of cysteine in the presence of other naturally occurring amino acids. Biochem J 104:627–633. https://doi.org/10.1042/bj1040627
doi: 10.1042/bj1040627 pubmed: 6048802 pmcid: 1270629
Garay LA, Boundy-Mills KL, German JB (2014) Accumulation of high-value lipids in single-cell microorganisms: a mechanistic approach and future perspectives. J Agric Food Chem 62:2709–2727. https://doi.org/10.1021/jf4042134
doi: 10.1021/jf4042134 pubmed: 24628496 pmcid: 3983371
Gavini N, Tungtur S, Pulakat L (2006) Peptidyl-prolyl cis/trans isomerase-independent functional NifH mutant of Azotobacter vinelandii. J Bacteriol 188:6020–6025. https://doi.org/10.1128/JB.00379-06
doi: 10.1128/JB.00379-06 pubmed: 16885471 pmcid: 1540071
Giannopolitis CN, Ries SK (1977) Superoxide Dismutases I. Occurrence in higher plants. Plant Physiol 59:309–314. https://doi.org/10.1104/pp.59.2.309
doi: 10.1104/pp.59.2.309 pubmed: 16659839 pmcid: 542387
Giovannelli D, Sievert SM, Hügler M, Markert S, Becher D, Schweder T, Vetriani C (2017) Insight into the evolution of microbial metabolism from the deep-branching bacterium. Thermovibrio Ammonificans Elife 6:e18990. https://doi.org/10.7554/eLife.18990
doi: 10.7554/eLife.18990 pubmed: 28436819
Goh KM, Kahar UM, Chai YY, Chong CS, Chai KP, Ranjani V, Illias RM, Chan KG (2013) Recent discoveries and applications of Anoxybacillus. Appl Microbiol Biotechnol 97:1475–1488. https://doi.org/10.1007/s00253-012-4663-2
doi: 10.1007/s00253-012-4663-2 pubmed: 23324802
Goodwine J, Gil J, Doiron A, Valdes J, Solis M, Higa A, Davis S, Sauer K (2019) Pyruvate-depleting conditions induce biofilm dispersion and enhance the efficacy of antibiotics in killing biofilms in vitro and in vivo. Sci Rep 9:3763. https://doi.org/10.1038/s41598-019-40378-z
doi: 10.1038/s41598-019-40378-z pubmed: 30842579 pmcid: 6403282
Guo H, Suzuki T, Rubinstein JL (2019) Structure of a bacterial ATP synthase. Elife 8:e43128. https://doi.org/10.7554/eLife.43128
doi: 10.7554/eLife.43128 pubmed: 30724163 pmcid: 6377231
Habig WH, Pabst MJ, Jakoby WB (1974) Glutathione S-transferases: the first enzymatic step in mercapturic acid formation. J Biol Chem 249:7130–7139. https://doi.org/10.1016/S0021-9258(19)42083-8
doi: 10.1016/S0021-9258(19)42083-8 pubmed: 4436300
Hamon MA, Stanley NR, Britton RA, Grossman AD, Lazazzera BA (2004) Identification of AbrB-regulated genes involved in biofilm formation by Bacillus subtilis. Mol Microbiol 52:847–860. https://doi.org/10.1111/j.1365-2958.2004.04023.x
doi: 10.1111/j.1365-2958.2004.04023.x pubmed: 15101989 pmcid: 1409746
Hayat S, Hayat Q, Alyemeni MN, Wani AS, Pichtel J, Ahmad A (2012) Role of proline under changing environments: a review. Plant Signal Behav 7:1456–1466. https://doi.org/10.4161/psb.21949
doi: 10.4161/psb.21949 pubmed: 22951402 pmcid: 3548871
Heath RL, Packer L (1968) Photoperoxidation in isolated chloroplasts. Arch Biochem Biophys 125:189–198. https://doi.org/10.1016/0003-98616890654-1
doi: 10.1016/0003-98616890654-1 pubmed: 5655425
Hederstedt L (2022) Diversity of cytochrome c oxidase assembly proteins in bacteria. Microorganisms 10:926. https://doi.org/10.3390/microorganisms10050926
doi: 10.3390/microorganisms10050926 pubmed: 35630371 pmcid: 9145763
Hibi T, Nii H, Nakatsu T, Kimura A, Kato H, Hiratake J, Oda JI (2004) Crystal structure of γ-glutamylcysteine synthetase: insights into the mechanism of catalysis by a key enzyme for glutathione homeostasis. Proc Natl Acad Sci USA 101:15052–15057. https://doi.org/10.1073/pnas.0403277101
doi: 10.1073/pnas.0403277101 pubmed: 15477603 pmcid: 523444
Hołówka J, Zakrzewska-Czerwińska J (2020) Nucleoid associated proteins: the small organizers that help to cope with stress. Front Microbiol 11:1–7. https://doi.org/10.3389/fmicb.2020.00590
doi: 10.3389/fmicb.2020.00590
Hor L, Dobson RC, Downton MT, Wagner J, Hutton CA, Perugini MA (2013) Dimerization of bacterial diaminopimelate epimerase is essential for catalysis. J Biol Chem 288:9238–9248. https://doi.org/10.1074/jbc.M113.450148
doi: 10.1074/jbc.M113.450148 pubmed: 23426375 pmcid: 3610995
Hryvusevich P, Navaselsky I, Talkachova Y, Straltsova D, Keisham M, Viatoshkin A, Samokhina V, Smolich I, Sokolik A, Huang X, Yu M, Bhatla SC, Demidchik V (2021) Sodium influx and potassium efflux currents in sunflower root cells under high salinity. Front Plant Sci 11:613936. https://doi.org/10.3389/fpls.2020.613936
doi: 10.3389/fpls.2020.613936 pubmed: 33537049 pmcid: 7848100
Huang Q, Zhang Z, Liu Q et al (2021) SpoVG is an important regulator of sporulation and affects biofilm formation by regulating Spo0A transcription in Bacillus cereus 0–9. BMC Microbiol 21:172. https://doi.org/10.1186/s12866-021-02239-6
doi: 10.1186/s12866-021-02239-6 pubmed: 34102998 pmcid: 8186074
Hughes L, Roberts W, Johnson D (2021) The impact of DNA adenine methyltransferase knockout on the development of triclosan resistance and antibiotic cross-resistance in Escherichia coli. Access Microbiol 3:acmi000178. https://doi.org/10.1099/acmi.0.000178
doi: 10.1099/acmi.0.000178 pubmed: 33997609
Ighodaro OM, Akinloye OA (2018) First line defence antioxidants-superoxide dismutase (SOD), catalase (CAT) and glutathione peroxidase (GPX): their fundamental role in the entire antioxidant defence grid. Alexandria J Med 54:287–293. https://doi.org/10.1016/j.ajme.2017.09.001
doi: 10.1016/j.ajme.2017.09.001
Jaiswal TP, Chakraborty S, Sharma S, Mishra A, Mishra AK, Singh SS (2023) Prospects of a hot spring-originated novel cyanobacterium, Scytonema ambikapurensis, for wastewater treatment and exopolysaccharide-enriched biomass production. Environ Sci Pollut Res 30:53424–53444. https://doi.org/10.1007/s11356-023-26032-2
doi: 10.1007/s11356-023-26032-2
Jordan S, Hutchings MI, Mascher T (2008) Cell envelope stress response in Gram-positive bacteria. FEMS Microbiol Rev 32:107–146. https://doi.org/10.1111/j.1574-6976.2007.00091.x
doi: 10.1111/j.1574-6976.2007.00091.x pubmed: 18173394
Juan CA, Pérez de la Lastra JM, Plou FJ, Pérez-Lebeña E (2021) The chemistry of reactive oxygen species (ROS) revisited: outlining their role in biological macromolecules (DNA, lipids and proteins) and induced pathologies. Int J Mol Sci 22:4642. https://doi.org/10.3390/ijms22094642
doi: 10.3390/ijms22094642 pubmed: 33924958 pmcid: 8125527
Kamashev D, Rouviere-Yaniv J (2000) The histone-like protein HU binds specifically to DNA recombination and repair intermediates. EMBO J 19:6527–6535. https://doi.org/10.1093/emboj/19.23.6527
doi: 10.1093/emboj/19.23.6527 pubmed: 11101525 pmcid: 305869
Karygianni L, Ren Z, Koo H, Thurnheer T (2020) Biofilm matrixome: extracellular components in structured microbial communities. Trends Microbiol 28:668–681. https://doi.org/10.1016/j.tim.2020.03.016
doi: 10.1016/j.tim.2020.03.016 pubmed: 32663461
Kasting JF (2016) Atmospheric composition of Hadean early Archean earth: The importance of CO. Geol Soc Am Spec 504:19–28. https://doi.org/10.1130/2014.2504(05)
doi: 10.1130/2014.2504(05)
Kimata K, Tanaka Y, Inada T, Aiba H (2001) Expression of the glucose transporter gene, ptsG, is regulated at the mRNA degradation step in response to glycolytic flux in Escherichia coli. EMBO J 20:3587–3595. https://doi.org/10.1093/emboj/20.13.3587
doi: 10.1093/emboj/20.13.3587 pubmed: 11432845 pmcid: 125514
Kitamura Y, Ebihara A, Agari Y, Shinkai A, Hirotsu K, Kuramitsu S (2009) Structure of D-alanine-D-alanine ligase from Thermus thermophilus HB8: cumulative conformational change and enzyme-ligand interactions. Acta Crystallogr D Biol Crystallogr 65:1098–1106. https://doi.org/10.1107/S0907444909029710
doi: 10.1107/S0907444909029710 pubmed: 19770507 pmcid: 2756165
Koga Y (2012) Thermal adaptation of the archaeal and bacterial lipid membranes. Archaea 2012:1–6. https://doi.org/10.1155/2012/789652
doi: 10.1155/2012/789652
Kosznik-Kwaśnicka K, Stasiłojć M, Grabowski Ł, Zdrojewska K, Węgrzyn G, Węgrzyn A (2022) Efficacy and safety of phage therapy against Salmonella enterica serovars Typhimurium and Enteritidis estimated by using a battery of in vitro tests and the Galleria mellonella animal model. Microbiol Res 261:127052. https://doi.org/10.1016/j.micres.2022.127052
doi: 10.1016/j.micres.2022.127052 pubmed: 35533436
Kühnl J, Bobik T, Procter JB, Burmeister C, Höppner J, Wilde I, Lüersen K, Torda AE, Walter RD, Liebau E (2005) Functional analysis of the methylmalonyl-CoA epimerase from Caenorhabditis elegans. FEBS J 272:1465–1477. https://doi.org/10.1111/j.1742-4658.2005.04579.x
doi: 10.1111/j.1742-4658.2005.04579.x pubmed: 15752362
Laksanalamai P, Robb FT (2004) Small heat shock proteins from extremophiles: a review. Extremophiles 8:1–11. https://doi.org/10.1007/s00792-003-0362-3
doi: 10.1007/s00792-003-0362-3 pubmed: 15064984
Lemmer KC, Dohnalkova AC, Noguera DR, Donohue TJ (2015) Oxygen-dependent regulation of bacterial lipid production. J Bacteriol 197:1649–1658. https://doi.org/10.1128/jb.02510-14
doi: 10.1128/jb.02510-14 pubmed: 25733615 pmcid: 4403652
Leng H, Wang Y, Zhao W, Sievert SM, Xiao X (2022) An expanded deep-branching thermophilic bacterial clade sheds light on the early evolution of bacteria. bioRxiv. https://doi.org/10.1101/2022.06.14.494929
doi: 10.1101/2022.06.14.494929
Levis NA, Pfennig DW (2020) Plasticity-led evolution: a survey of developmental mechanisms and empirical tests. Evol Dev 22:71–87. https://doi.org/10.1111/ede.12309
doi: 10.1111/ede.12309 pubmed: 31449722
Limoli DH, Jones CJ, Wozniak DJ (2015) Bacterial extracellular polysaccharides in biofilm formation and function. Microbiol Spectr. https://doi.org/10.1128/microbiolspec.MB-0011-2014
doi: 10.1128/microbiolspec.MB-0011-2014 pubmed: 26185074
Lindqvist R, Barmark G (2014) Specific growth rate determines the sensitivity of Escherichia coli to lactic acid stress: implications for predictive microbiology. Biomed Res Int 2014:471317. https://doi.org/10.1155/2014/471317
doi: 10.1155/2014/471317 pubmed: 25110680 pmcid: 4109666
Liu B, Qian SB (2014) Translational reprogramming in cellular stress response. Wiley Interdiscip Rev RNA 5:301–305. https://doi.org/10.1002/wrna.1212
doi: 10.1002/wrna.1212 pubmed: 24375939
Livak KJ, Schmittgen TD (2001) Analysis of relative gene expression data using real-time quantitative PCR and the 2
doi: 10.1006/meth.2001.1262 pubmed: 11846609
Loh PC, Morimoto T, Matsuo Y, Oshima T, Ogasawara N (2007) The GTP-binding protein YqeH participates in biogenesis of the 30S ribosome subunit in Bacillus subtilis. Genes Genet Syst 82:281–289. https://doi.org/10.1266/ggs.82.281
doi: 10.1266/ggs.82.281 pubmed: 17895579
Loreto F, Velikova V (2001) Isoprene produced by leaves protects the photosynthetic apparatus against ozone damage, quenches ozone products, and reduces lipid peroxidation of cellular membranes. Plant Physiol 127:1781–1787. https://doi.org/10.1104/pp.010497
doi: 10.1104/pp.010497 pubmed: 11743121 pmcid: 133581
Lovegrove A, Edwards CH, De Noni I, Patel H, El SN, Grassby T, Zielke C, Ulmius M, Nilsson L, Butterworth PJ, Ellis PR, Shewry PR (2017) Role of polysaccharides in food, digestion, and health. Crit Rev Food Sci Nutr 57:237–253. https://doi.org/10.1080/10408398.2014.939263
doi: 10.1080/10408398.2014.939263 pubmed: 25921546
Lusk BG (2019) Thermophiles; or, the modern prometheus: the importance of extreme microorganisms for understanding and applying extracellular electron transfer. Front Microbiol 10:818. https://doi.org/10.3389/fmicb.2019.00818
doi: 10.3389/fmicb.2019.00818 pubmed: 31080440 pmcid: 6497744
Macdonald Ighodaro O, Mohammed Adeosun A, Adeboye Akinloye O (2017) Alloxan-induced diabetes, a common model for evaluating the glycemic-control potential of therapeutic compounds and plants extracts in experimental studies. Medicina 53:365–374. https://doi.org/10.1016/j.medici.2018.02.001
doi: 10.1016/j.medici.2018.02.001 pubmed: 29548636
Mangan MW, Lucchini S, Ócróinín T, Fitzgerald S, Hinton JC, Dorman CJ (2011) Nucleoid-associated protein HU controls three regulons that coordinate virulence, response to stress and general physiology in Salmonella enterica serovar Typhimurium. Microbiology 157:1075–1087. https://doi.org/10.1099/mic.0.046359-0
doi: 10.1099/mic.0.046359-0 pubmed: 21212121
Marchetti M, Malinowska A, Heller I, Wuite GJL (2017) How to switch the motor on: RNA polymerase initiation steps at the single-molecule level. Protein Sci 26:1303–1313. https://doi.org/10.1002/pro.3183
doi: 10.1002/pro.3183 pubmed: 28470684 pmcid: 5477531
Maslowska KH, Makiela-Dzbenska K, Fijalkowska IJ (2019) The SOS system: A complex and tightly regulated response to DNA damage. Environ Mol Mutagen 60:368–384. https://doi.org/10.1002/em.22267
doi: 10.1002/em.22267 pubmed: 30447030 pmcid: 6590174
Massengo-Tiassé RP, Cronan JE (2009) Diversity in enoyl-acyl carrier protein reductases. Cell Mol Life Sci 66:1507–1517. https://doi.org/10.1007/s00018-009-8704-7
doi: 10.1007/s00018-009-8704-7 pubmed: 19151923 pmcid: 2819910
Menghini S, Ho PS, Gwisai T, Schuerle S (2021) Magnetospirillum magneticum as a living iron chelator induces TfR1 upregulation and decreases cell viability in cancer cells. Int J Mol Sci 22:1–12. https://doi.org/10.3390/ijms22020498
doi: 10.3390/ijms22020498
Mengin-Lecreulx D, van Heijenoort J (1994) Copurification of glucosamine-1-phosphate acetyltransferase and N-acetylglucosamine-1-phosphate uridyltransferase activities of Escherichia coli: characterization of the glmU gene product as a bifunctional enzyme catalyzing two subsequent steps in the pathway for UDP-N-acetylglucosamine synthesis. J Bacteriol 176:5788–5795. https://doi.org/10.1128/jb.176.18.5788-5795.1994
doi: 10.1128/jb.176.18.5788-5795.1994 pubmed: 8083170 pmcid: 196783
Mihara H, Esaki N (2002) Bacterial cysteine desulfurases: their function and mechanisms. Appl Microbiol Biotechnol 60:12–23. https://doi.org/10.1007/s00253-002-1107-4
doi: 10.1007/s00253-002-1107-4 pubmed: 12382038
Mika A, Lüthje S (2003) Properties of guaiacol peroxidase activities isolated from corn root plasma membranes. Plant Physiol 132:1489–1498. https://doi.org/10.1104/pp.103.020396
doi: 10.1104/pp.103.020396 pubmed: 12857829 pmcid: 167087
Milojevic T, Cramm MA, Hubert CR, Westall F (2022) “Freezing” thermophiles: from one temperature extreme to another. Microorganisms 10:2417. https://doi.org/10.3390/microorganisms10122417
doi: 10.3390/microorganisms10122417 pubmed: 36557670 pmcid: 9782878
Mishra A, Kesarwani S, Jaiswal TP, Bhattacharjee S, Chakraborty S, Mishra AK, Singh SS (2023) Decoding whole genome of Anoxybacillus rupiensis TPH1 isolated from tatapani hot spring, India and giving insight into bioremediation ability of TPH1 via heavy metals and azo dyes. Res Microbiol 174:104027. https://doi.org/10.1016/j.resmic.2023.104027
doi: 10.1016/j.resmic.2023.104027 pubmed: 36646262
Mogk A, Deuerling E, Vorderwülbecke S, Vierling E, Bukau B (2003) Small heat shock proteins, ClpB and the DnaK system form a functional triade in reversing protein aggregation. Mol Microbiol 50:585–595. https://doi.org/10.1046/j.1365-2958.2003.03710.x
doi: 10.1046/j.1365-2958.2003.03710.x pubmed: 14617181
Mohammad BT, Al Daghistani HI, Jaouani A, Abdel-Latif S, Kennes C (2017) Isolation and characterization of thermophilic bacteria from Jordanian hot springs: Bacillus licheniformis and Thermomonas hydrothermalis isolates as potential producers of thermostable enzymes. Int J Microbiol. https://doi.org/10.1155/2017/6943952
doi: 10.1155/2017/6943952 pubmed: 29163641 pmcid: 5661075
Mohammed ASA, Naveed M, Jost N (2021) Polysaccharides; classification, chemical properties, and future perspective applications in fields of pharmacology and biological medicine (A review of current applications and upcoming potentialities). J Polym Environ 29:2359–2371. https://doi.org/10.1007/s10924-021-02052-2
doi: 10.1007/s10924-021-02052-2 pubmed: 33526994 pmcid: 7838237
Mohedano ML, Overweg K, de la Fuente A, Reuter M, Altabe S, Mulholland F, de Mendoza D, López P, Wells JM (2005) Evidence that the essential response regulator YycF in Streptococcus pneumoniae modulates expression of fatty acid biosynthesis genes and alters membrane composition. J Bacteriol 187:2357–2367. https://doi.org/10.1128/JB.187.7.2357-2367.2005
doi: 10.1128/JB.187.7.2357-2367.2005 pubmed: 15774879 pmcid: 1065234
Neupane P, Bhuju S, Thapa N, Bhattarai HK (2019) ATP synthase: structure, function and inhibition. Biomol Concepts 10:1–10. https://doi.org/10.1515/bmc-2019-0001
doi: 10.1515/bmc-2019-0001 pubmed: 30888962
Newcomb ES, Douma LG, Morris LA, Bloom LB (2022) The Escherichia coli clamp loader rapidly remodels SSB on DNA to load clamps. Nucleic Acids Res 50:12872–12884. https://doi.org/10.1093/nar/gkac1169
doi: 10.1093/nar/gkac1169 pubmed: 36511874 pmcid: 9825162
Nowak E, Jaciuk M, Skowronek K, Tańska A, Nowotny M (2012) Structure of UvrA nucleotide excision repair protein in complex with modified DNA. Acta Crystallogr A 68:s142–s142. https://doi.org/10.1107/S0108767312097279
doi: 10.1107/S0108767312097279
Orlowski M, Meister A (1971) Partial reactions catalyzed by -glutamylcysteine synthetase and evidence for an activated glutamate intermediate. J Biol Chem 246:7095–7105. https://doi.org/10.1016/s0021-92581945858-4
doi: 10.1016/s0021-92581945858-4 pubmed: 4256952
Parrilli E, Tutino ML, Marino G (2022) Biofilm as an adaptation strategy to extreme conditions. Rend Lincei Sci Fis Nat 33:527–536. https://doi.org/10.1007/s12210-022-01083-8
doi: 10.1007/s12210-022-01083-8
Pavithra K, Vadivukkarasi S (2015) Evaluation of free radical scavenging activity of various extracts of leaves from Kedrostis foetidissima (Jacq.) Cogn. Food Sci Hum Wellness 4:42–46. https://doi.org/10.1016/j.fshw.2015.02.001
doi: 10.1016/j.fshw.2015.02.001
Perez E, Rubio MB, Cardoza RE, Gutierrez S, Bettiol W, Monte E, Hermosa R (2015) The importance of chorismate mutase in the biocontrol potential of Trichoderma parareesei. Front Microbiol 6:1181. https://doi.org/10.3389/fmicb.2015.01181
doi: 10.3389/fmicb.2015.01181 pubmed: 26579090 pmcid: 4621298
Perron NR, Brumaghim JL (2009) A review of the antioxidant mechanisms of polyphenol compounds related to iron binding. Cell Biochem Biophys 53:75–100. https://doi.org/10.1007/s12013-009-9043-x
doi: 10.1007/s12013-009-9043-x pubmed: 19184542
Qayyum MZ, Dey D, Sen R (2016) Transcription elongation factor NusA is a general antagonist of rho-dependent termination in Escherichia coli. J Biol Chem 291:8090–8108. https://doi.org/10.1074/jbc.M115.701268
doi: 10.1074/jbc.M115.701268 pubmed: 26872975 pmcid: 4825012
Ratnayake WM (2015) Concerns about the use of 15:0, 17:0, and trans-16:1n–7 as biomarkers of dairy fat intake in recent observational studies that suggest beneficial effects of dairy food on incidence of diabetes and stroke. Am J Clin Nutr 101:1102–1103. https://doi.org/10.3945/ajcn.114.105379
doi: 10.3945/ajcn.114.105379 pubmed: 25934871 pmcid: 4409693
Reniere ML (2018) Reduce, induce, thrive: bacterial redox sensing during pathogenesis. J Bacteriol 200:e00128-e218. https://doi.org/10.1128/JB.00128-18
doi: 10.1128/JB.00128-18 pubmed: 29891640 pmcid: 6088161
Rio DC, Ares M, Hannon GJ, Nilsen W (2010) Purification of RNA using TRIzol (TRI reagent). Cold Spring Harb Protoc. https://doi.org/10.1101/pdb.prot5439
doi: 10.1101/pdb.prot5439 pubmed: 20647358
Robbins-Manke JL, Zdraveski ZZ, Marinus M, Essigmann JM (2005) Analysis of global gene expression and double-strand-break formation in DNA adenine methyltransferase-and mismatch repair-deficient Escherichia coli. J Bacteriol 187:7027–7037. https://doi.org/10.1128/jb.187.20.7027-7037.2005
doi: 10.1128/jb.187.20.7027-7037.2005 pubmed: 16199573 pmcid: 1251628
Rohrwild M, Coux O, Huang HC, Moerschell RP, Yoo SJ, Seol JH, Chung CH, Goldberg AL (1996) HslV-HslU: A novel ATP-dependent protease complex in Escherichia coli related to the eukaryotic proteasome. Proc Nat Acad Sci USA 93:5808–5813. https://doi.org/10.1073/pnas.93.12.5808
doi: 10.1073/pnas.93.12.5808 pubmed: 8650174 pmcid: 39143
Samadpour AN, Merrikh H (2018) DNA gyrase activity regulates DnaA-dependent replication initiation in Bacillus subtilis. Mol Microbiol 108:115–127. https://doi.org/10.1111/mmi.13920
doi: 10.1111/mmi.13920 pubmed: 29396913 pmcid: 5893406
Schaedle M, Bassham JA (1977) Chloroplast glutathione reductase. Plant Physiol 59:1011–1012. https://doi.org/10.1104/pp.59.5.1011
doi: 10.1104/pp.59.5.1011 pubmed: 16659940 pmcid: 543356
Schirrmeister BE, de Vos JM, Antonelli A, Bagheri HC (2013) Evolution of multicellularity coincided with increased diversification of cyanobacteria and the Great Oxidation Event. Proc Nat Acad Sci USA 110:1791–1796. https://doi.org/10.1073/pnas.1209927110
doi: 10.1073/pnas.1209927110 pubmed: 23319632 pmcid: 3562814
Schlagman SL, Hattman S, Marinus MG (1986) Direct role of the Escherichia coli Dam DNA methyltransferase in methylation-directed mismatch repair. J Bacteriol 165:896–900. https://doi.org/10.1128/jb.165.3.896-900.1986
doi: 10.1128/jb.165.3.896-900.1986 pubmed: 3512529 pmcid: 214513
Sedlak J, Lindsay RH (1968) Estimation of total, protein-bound, and nonprotein sulfhydryl groups in tissue with Ellman’s reagent. Anal Biochem 25:192–205. https://doi.org/10.1016/0003-26976890092-4
doi: 10.1016/0003-26976890092-4 pubmed: 4973948
Seixas AF, Quendera AP, Sousa JP, Silva AF, Arraiano CM, Andrade JM (2022) Bacterial response to oxidative stress and RNA oxidation. Front Genet 12:821535. https://doi.org/10.3389/fgene.2021.821535
doi: 10.3389/fgene.2021.821535 pubmed: 35082839 pmcid: 8784731
Sharma S, Vaid S, Bhat B, Singh S, Bajaj BK (2019) Thermostable enzymes for industrial biotechnology. Adv Enzyme Technol. https://doi.org/10.1016/B978-0-444-64114-4.00017-0
doi: 10.1016/B978-0-444-64114-4.00017-0
Sies H (2021) Oxidative eustress: On constant alert for redox homeostasis. Redox Biol 41:101867. https://doi.org/10.1016/j.redox.2021.101867
doi: 10.1016/j.redox.2021.101867 pubmed: 33657525 pmcid: 7930632
Silas Y, Singer E, Das K, Lehming N, Pines O (2021) A combination of Class-I fumarases and metabolites (α-ketoglutarate and fumarate) signal the DNA damage response in Escherichia coli. Proc Natl Acad Sci U S A 118:e2026595118. https://doi.org/10.1073/pnas.2026595118
doi: 10.1073/pnas.2026595118 pubmed: 34083440 pmcid: 8201922
Silva JME, Martins LHDS, Moreira DKT, Silva LDP, Barbosa PPM, Komesu A, Ferreira NR, Oliveira JAR (2023) Microbial lipid based biorefinery concepts: a review of status and prospects. Foods 12(10):2074. https://doi.org/10.3390/foods12102074
doi: 10.3390/foods12102074
Singh H, Dai Y, Outten FW, Busenlehner LS (2013) Escherichia coli SufE sulfur transfer protein modulates the SufS cysteine desulfurase through allosteric conformational dynamics. J Biol Chem 288:36189–36200. https://doi.org/10.1074/jbc.M113.525709
doi: 10.1074/jbc.M113.525709 pubmed: 24196966 pmcid: 3868733
Singh DP, Prabha R, Verma S, Meena KK, Yandigeri M (2017) Antioxidant properties and polyphenolic content in terrestrial cyanobacteria. 3 Biotech 7:1–14. https://doi.org/10.1007/s13205-017-0786-6
doi: 10.1007/s13205-017-0786-6
Singh VK, Sirobhushanam S, Ring RP, Singh S, Gatto C, Wilkinson BJ (2018) Roles of pyruvate dehydrogenase and branched-chain α-keto acid dehydrogenase in branched-chain membrane fatty acid levels and associated functions in Staphylococcus aureus. J Med Microbiol 67:570–578. https://doi.org/10.1099/jmm.0.000707
doi: 10.1099/jmm.0.000707 pubmed: 29498620 pmcid: 5982145
Solmi L, Rossi FR, Romero FM, Bach-Pages M, Preston GM, Ruiz OA, Gárriz A (2023) Polyamine-mediated mechanisms contribute to oxidative stress tolerance in Pseudomonas syringae. Sci Rep 13:4279. https://doi.org/10.1038/s41598-023-31239-x
doi: 10.1038/s41598-023-31239-x pubmed: 36922543 pmcid: 10017717
Song Y, Leonard SW, Traber MG, Ho E (2009) Zinc deficiency affects DNA damage, oxidative stress, antioxidant defenses, and DNA repair in rats. J Nutr 139:1626–1631. https://doi.org/10.3945/jn.109.106369
doi: 10.3945/jn.109.106369 pubmed: 19625698 pmcid: 3151020
Soutourina O, Poupel O, Coppée JY, Danchin A, Msadek T, Martin-Verstraete I (2009) CymR, the master regulator of cysteine metabolism in Staphylococcus aureus, controls host sulphur source utilization and plays a role in biofilm formation. Mol Microbiol 73:194–211. https://doi.org/10.1111/j.1365-2958.2009.06760.x
doi: 10.1111/j.1365-2958.2009.06760.x pubmed: 19508281
Staerck C, Gastebois A, Vandeputte P, Calenda A, Larcher G, Gillmann L, Papon N, Bouchara JP, Fleury MJ (2017) Microbial antioxidant defense enzymes. Microb Pathog 110:56–65. https://doi.org/10.1016/j.micpath.2017.06.015
doi: 10.1016/j.micpath.2017.06.015 pubmed: 28629723
Stauffer ME, Young JK, Helms GL, Evans JN (2001) Chemical shift mapping of shikimate-3-phosphate binding to the isolated N-terminal domain of 5-enolpyruvylshikimate-3-phosphate synthase. FEBS Lett 499:182–186. https://doi.org/10.1016/S0014-5793(01)02555-8
doi: 10.1016/S0014-5793(01)02555-8 pubmed: 11418136
Stincone A, Prigione A, Cramer T, Wamelink MM, Campbell K, Cheung E, Olin-Sandoval V, Grüning NM, Krüger A, Tauqeer Alam M, Keller MA, Breitenbach M, Brindle KM, Rabinowitz JD, Ralser M (2015) The return of metabolism: biochemistry and physiology of the pentose phosphate pathway. Biol Rev Camb Philos Soc 90:927–963. https://doi.org/10.1111/brv.12140
doi: 10.1111/brv.12140 pubmed: 25243985
Su YB, Peng B, Li H, Cheng ZX, Zhang TT, Zhu JX, Li D, Li MY, Ye JZ, Du CC, Zhang S (2018) Pyruvate cycle increases aminoglycoside efficacy and provides respiratory energy in bacteria. Proc Natl Acad Sci USA 115:E1578–E1587. https://doi.org/10.1073/pnas.1714645115
doi: 10.1073/pnas.1714645115 pubmed: 29382755 pmcid: 5816162
Sulthana S, Quesada E, Deutscher MP (2017) RNase II regulates RNase PH and is essential for cell survival during starvation and stationary phase. RNA 23:1456–1464. https://doi.org/10.1261/rna.060558.116
doi: 10.1261/rna.060558.116 pubmed: 28625967 pmcid: 5558914
Townsend DM, Tew KD (2003) The role of glutathione-S-transferase in anti-cancer drug resistance. Oncogene 22:7369–7375. https://doi.org/10.1038/sj.onc.1206940
doi: 10.1038/sj.onc.1206940 pubmed: 14576844 pmcid: 6361125
Tsao R (2010) Chemistry and biochemistry of dietary polyphenols. Nutrients 2:1231–1246. https://doi.org/10.3390/nu2121231
doi: 10.3390/nu2121231 pubmed: 22254006 pmcid: 3257627
Ueta M, Ohniwa RL, Yoshida H, Maki Y, Wada C, Wada A (2008) Role of HPF (hibernation promoting factor) in translational activity in Escherichia coli. J Biochem 143:425–433. https://doi.org/10.1093/jb/mvm243
doi: 10.1093/jb/mvm243 pubmed: 18174192
Van Handel E (1985) Rapid determination of total lipids in mosquitoes. J Am Mosq Control Assoc 1:302–304
pubmed: 2906672
Vandieken V, Knoblauch C, Jørgensen BB (2006) Desulfotomaculum arcticum sp. nov., a novel spore-forming, moderately thermophilic, sulfate-reducing bacterium isolated from a permanently cold fjord sediment of Svalbard. Int J Syst Evol Microbiol 56:687–690. https://doi.org/10.1099/ijs.0.64058-0
doi: 10.1099/ijs.0.64058-0 pubmed: 16585677
Vargas-Blanco DA, Shell SS (2020) Regulation of mRNA stability during bacterial stress responses. Front Microbiol 11:2111. https://doi.org/10.3389/fmicb.2020.02111
doi: 10.3389/fmicb.2020.02111 pubmed: 33013770 pmcid: 7509114
Venn-Watson SK, Butterworth CN (2022) Broader and safer clinically-relevant activities of pentadecanoic acid compared to omega-3: evaluation of an emerging essential fatty acid across twelve primary human cell-based disease systems. PLoS One 17:e0268778. https://doi.org/10.1371/journal.pone.0268778
doi: 10.1371/journal.pone.0268778 pubmed: 35617322 pmcid: 9135213
Venn-Watson SK, Lumpkin R, Dennis EA (2020) Efficacy of dietary odd-chain saturated fatty acid pentadecanoic acid parallels broad associated health benefits in humans: could it be essential? Sci Rep 10:8161. https://doi.org/10.1038/s41598-020-64960-y
doi: 10.1038/s41598-020-64960-y pubmed: 32424181 pmcid: 7235264
Vinçon-Laugier A, Cravo-Laureau C, Mitteau I, Grossi V (2017) Temperature-dependent alkyl glycerol ether lipid composition of mesophilic and thermophilic sulfate-reducing bacteria. Front Microbiol 8:1532. https://doi.org/10.3389/fmicb.2017.01532
doi: 10.3389/fmicb.2017.01532 pubmed: 28848536 pmcid: 5552659
Walker JC (1978) The early history of oxygen and ozone in the atmosphere. Pure Appl Geophys 117:498–512. https://doi.org/10.1007/BF00876630
doi: 10.1007/BF00876630
Wang AG, Luo GH (1990) Quantitative relation between the reaction of hydroxylamine and superoxide anion radicals in plants. Plant Physiol Commun 26:55–57
Wang Q, Cen Z, Zhao J (2015) The survival mechanisms of thermophiles at high temperatures: an angle of omics. Physiology 30:97–106. https://doi.org/10.1152/physiol.00066.2013
doi: 10.1152/physiol.00066.2013 pubmed: 25729055
Wang Y, Han H, Cui B, Hou Y, Wang Y, Wang Q (2017) A glutathione peroxidase from Antarctic psychrotrophic bacterium Pseudoalteromonas sp. ANT506: Cloning and heterologous expression of the gene and characterization of recombinant enzyme. Bioengineered 8:742–749. https://doi.org/10.1080/21655979.2017.1373534
doi: 10.1080/21655979.2017.1373534 pubmed: 28873004 pmcid: 5736345
Warrilow AG, Hawkesford MJ (2000) Cysteine synthase (O-acetylserine (thiol) lyase) substrate specificities classify the mitochondrial isoform as a cyanoalanine synthase. J Exp Bot 51:985–993. https://doi.org/10.1093/jexbot/51.347.985
doi: 10.1093/jexbot/51.347.985 pubmed: 10948226
Whitley KD, Jukes C, Tregidgo N, Karinou E, Almada P, Cesbron Y, Henriques R, Dekker C, Holden S (2021) FtsZ treadmilling is essential for Z-ring condensation and septal constriction initiation in Bacillus subtilis cell division. Nat Commun 12:2448. https://doi.org/10.1038/s41467-021-22526-0
doi: 10.1038/s41467-021-22526-0 pubmed: 33907196 pmcid: 8079713
Wyrzykowski J, Volkert MR (2003) The Escherichia coli methyl-directed mismatch repair system repairs base pairs containing oxidative lesions. J Bacteriol 185:1701–1704. https://doi.org/10.1128/jb.185.5.1701-1704.2003
doi: 10.1128/jb.185.5.1701-1704.2003 pubmed: 12591888 pmcid: 148063
Xun Z, Sowell RA, Kaufman TC, Clemmer DE (2007) Protein expression in a Drosophila model of Parkinson’s disease. J Proteome Res 6:348–357. https://doi.org/10.1021/pr060488o
doi: 10.1021/pr060488o pubmed: 17203978 pmcid: 2597372
Yeh JI, Chinte U, Du S (2008) Structure of glycerol-3-phosphate dehydrogenase, an essential monotopic membrane enzyme involved in respiration and metabolism. Proc Natl Acad Sci USA 105:3280–3285. https://doi.org/10.1073/pnas.0712331105
doi: 10.1073/pnas.0712331105 pubmed: 18296637 pmcid: 2265192
Yin YG, Kobayashi Y, Sanuki A, Kondo S, Fukuda N, Ezura H, Sugaya S, Matsukura C (2010) Salinity induces carbohydrate accumulation and sugar-regulated starch biosynthetic genes in tomato (Solanum lycopersicum L. cv. ‘Micro-Tom’) fruits in an ABA-and osmotic stress-independent manner. J Exp Botany 61:563–574. https://doi.org/10.1093/jxb/erp333
doi: 10.1093/jxb/erp333
Zagorchev L, Seal CE, Kranner I, Odjakova M (2013) A central role for thiols in plant tolerance to abiotic stress. I J Mol Sci 14:7405–7432. https://doi.org/10.3390/ijms14047405
doi: 10.3390/ijms14047405
Zahnle KJ, Lupu R, Catling DC, Wogan N (2020) Creation and evolution of impact-generated reduced atmospheres of early earth. Planet Sci J 1:11. https://doi.org/10.3847/PSJ/ab7e2c
doi: 10.3847/PSJ/ab7e2c
Zandi P, Schnug E (2022) Reactive oxygen species, antioxidant responses and implications from a microbial modulation perspective. Biology 11:155. https://doi.org/10.3390/biology11020155
doi: 10.3390/biology11020155 pubmed: 35205022 pmcid: 8869449
Zatakia HM, Arapov TD, Meier VM, Scharf BE (2018) Cellular stoichiometry of methyl-accepting chemotaxis proteins in Sinorhizobium meliloti. J Bacteriol 200:e00614-e617. https://doi.org/10.1128/JB.00614-17
doi: 10.1128/JB.00614-17 pubmed: 29263102 pmcid: 5826028
Zhang Y, Meng D, Wang Z, Guo H, Wang Y (2012) Oxidative stress response in two representative bacteria exposed to atrazine. FEMS Microbiol Lett 334:95–101. https://doi.org/10.1111/j.1574-6968.2012.02625.x
doi: 10.1111/j.1574-6968.2012.02625.x pubmed: 22724442
Zhang Y, Liu T, Li MM, Hua ZS, Evans P, Qu Y, Tan S, Zheng M, Lu H, Jiao JY, Lücker S (2023) Hot spring distribution and survival mechanisms of thermophilic comammox Nitrospira. ISME J 17:1–11. https://doi.org/10.1038/s41396-023-01409-w
doi: 10.1038/s41396-023-01409-w
Zhao X, Drlica K (2014) Reactive oxygen species and the bacterial response to lethal stress. Curr Opin Microbiol 21:1–6. https://doi.org/10.1016/j.mib.2014.06.008
doi: 10.1016/j.mib.2014.06.008 pubmed: 25078317
Zhou D, Tanzawa T, Lin J, Gagnon MG (2020) Structural basis for ribosome recycling by RRF and tRNA. Nat Struct Mol Biol 27:25–32. https://doi.org/10.1038/s41594-019-0350-7
doi: 10.1038/s41594-019-0350-7 pubmed: 31873307

Auteurs

Aditi Mishra (A)

Laboratory of Cyanobacterial Systematics and Stress Biology, Department of Botany, Banaras Hindu University, Varanasi, India.

Sindhunath Chakraborty (S)

Laboratory of Microbial Genetics, Department of Botany, Banaras Hindu University, Varanasi, India.

Tameshwar Prasad Jaiswal (TP)

Laboratory of Cyanobacterial Systematics and Stress Biology, Department of Botany, Banaras Hindu University, Varanasi, India.

Samujjal Bhattacharjee (S)

Laboratory of Microbial Genetics, Department of Botany, Banaras Hindu University, Varanasi, India.

Shreya Kesarwani (S)

Laboratory of Cyanobacterial Systematics and Stress Biology, Department of Botany, Banaras Hindu University, Varanasi, India.

Arun Kumar Mishra (AK)

Laboratory of Microbial Genetics, Department of Botany, Banaras Hindu University, Varanasi, India.

Satya Shila Singh (SS)

Laboratory of Cyanobacterial Systematics and Stress Biology, Department of Botany, Banaras Hindu University, Varanasi, India. satyashila@rediffmail.com.

Articles similaires

Photosynthesis Ribulose-Bisphosphate Carboxylase Carbon Dioxide Molecular Dynamics Simulation Cyanobacteria
Biofilms Candida albicans Quorum Sensing Candida glabrata Menthol
Animals Lung India Sheep Transcriptome
Silicon Dioxide Water Hot Temperature Compressive Strength X-Ray Diffraction

Classifications MeSH