Purification and ATPase Activity Measurement of Spiroplasma MreB.
Absorption spectroscopy
Bacterial actin cytoskeleton
E. coli expression system
Gel filtration
Ni2+-NTA affinity chromatography
Pi release assay
Recombinant protein
Journal
Methods in molecular biology (Clifton, N.J.)
ISSN: 1940-6029
Titre abrégé: Methods Mol Biol
Pays: United States
ID NLM: 9214969
Informations de publication
Date de publication:
2023
2023
Historique:
entrez:
26
2
2023
pubmed:
27
2
2023
medline:
3
3
2023
Statut:
ppublish
Résumé
Spiroplasma is a genus of wall-less helical bacteria with swimming motility unrelated to conventional types of bacterial motility machinery, such as flagella and pili. The swimming of Spiroplasma is suggested to be driven by five classes of MreB (MreB1-MreB5), which are members of the actin superfamily. In vitro studies of Spiroplasma MreBs have recently been conducted to evaluate their activities, such as ATPase, which is essential for the polymerization dynamics among classic actin superfamily proteins. In this chapter, we describe methods of purification and P
Identifiants
pubmed: 36842130
doi: 10.1007/978-1-0716-3060-0_30
doi:
Substances chimiques
Actins
0
Adenosine Triphosphatases
EC 3.6.1.-
Bacterial Proteins
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
359-371Informations de copyright
© 2023. The Author(s), under exclusive license to Springer Science+Business Media, LLC, part of Springer Nature.
Références
Paredes JC, Herren JK, Schüpfer F et al (2015) Genome sequence of the Drosophila melanogaster male-killing Spiroplasma strain MSRO endosymbiont. mBio 6(2):e02437–02414
Gasparich GE (2002) Spiroplasmas: evolution, adaptation and diversity. Front Biosci 7:d619–d640
pubmed: 11861210
Liu P, Zheng H, Meng Q et al (2017) Chemotaxis without conventional two-component system, based on cell polarity and aerobic conditions in helicity-switching swimming of Spiroplasma eriocheiris. Front Microbiol 8:58
pubmed: 28217108
pmcid: 5289999
Terahara N, Tulum I, Miyata M (2017) Transformation of crustacean pathogenic bacterium Spiroplasma eriocheiris and expression of yellow fluorescent protein. Biochem Biophys Res Commun 487(3):488–493
doi: 10.1016/j.bbrc.2017.03.144
pubmed: 28363870
Miyata M, Robinson RC, Uyeda TQP et al (2020) Tree of motility – a proposed history of motility systems in the tree of life. Genes Cells 25(1):6–21
doi: 10.1111/gtc.12737
pubmed: 31957229
pmcid: 7004002
Nakane D, Ito T, Nishizaka T (2020) Coexistence of two chiral helices produces kink translation in Spiroplasma swimming. J Bacteriol 202(8):e00735–e00719
doi: 10.1128/JB.00735-19
pubmed: 32041794
pmcid: 7099143
Shaevitz JW, Lee JY, Fletcher DA (2005) Spiroplasma swim by a processive change in body helicity. Cell 122(6):941–945
doi: 10.1016/j.cell.2005.07.004
pubmed: 16179261
Kiyama H, Kakizawa S, Sasajima Y et al (2022) Reconstitution of minimal motility system based on Spiroplasma swimming by two bacterial actins in a synthetic minimal bacterium. Sci Adv 8(48):eabo7490
Takahashi D, Fujiwara I, Miyata M (2020) Phylogenetic origin and sequence features of MreB from the wall-less swimming bacteria Spiroplasma. Biochem Biophys Res Commun 533(4):638–644
doi: 10.1016/j.bbrc.2020.09.060
pubmed: 33066960
Harne S, Duret S, Pande V et al (2020) MreB5 is a determinant of rod-to-helical transition in the cell-wall-less bacterium Spiroplasma. Curr Biol 30(23):4753–4762.e4757
Ku C, Lo WS, Kuo CH (2014) Molecular evolution of the actin-like MreB protein gene family in wall-less bacteria. Biochem Biophys Res Commun 446(4):927–932
doi: 10.1016/j.bbrc.2014.03.039
pubmed: 24650664
Trachtenberg S, Dorward LM, Speransky VV et al (2008) Structure of the cytoskeleton of Spiroplasma melliferum BC3 and its interactions with the cell membrane. J Mol Biol 378(4):778–789
doi: 10.1016/j.jmb.2008.02.020
pubmed: 18400234
Kürner J, Frangakis AS, Baumeister W (2005) Cryo-electron tomography reveals the cytoskeletal structure of Spiroplasma melliferum. Science 307(5708):436–438
doi: 10.1126/science.1104031
pubmed: 15662018
Shi H, Bratton BP, Gitai Z et al (2018) How to build a bacterial cell: MreB as the foreman of E. coli construction. Cell 172(6):1294–1305
doi: 10.1016/j.cell.2018.02.050
pubmed: 29522748
pmcid: 5846203
Wagstaff J, Löwe J (2018) Prokaryotic cytoskeletons: protein filaments organizing small cells. Nat Rev Microbiol 16(4):187–201
doi: 10.1038/nrmicro.2017.153
pubmed: 29355854
Takahashi D, Fujiwara I, Sasajima Y et al (2022) ATP-dependent polymerization dynamics of bacterial actin proteins involved in Spiroplasma swimming. Open Biol 12(10):220083
Wegner A (1976) Head to tail polymerization of actin. J Mol Biol 108(1):139–150
doi: 10.1016/S0022-2836(76)80100-3
pubmed: 1003481
Masson F, Pierrat X, Lemaitre B et al (2021) The wall-less bacterium Spiroplasma poulsonii builds a polymeric cytoskeleton composed of interacting MreB isoforms. iScience 24(12):103458
doi: 10.1016/j.isci.2021.103458
pubmed: 34888500
pmcid: 8634037
Pande V, Mitra N, Bagde SR et al (2022) Filament organization of the bacterial actin MreB is dependent on the nucleotide state. J Cell Biol 221(5):e202106092
doi: 10.1083/jcb.202106092
pubmed: 35377392
pmcid: 9195046
Blanchoin L, Pollard TD (1999) Mechanism of interaction of Acanthamoeba actophorin (ADF/cofilin) with actin filaments. J Biol Chem 274(22):15538–15546
doi: 10.1074/jbc.274.22.15538
pubmed: 10336448
Webb MR (1992) A continuous spectrophotometric assay for inorganic-phosphate and for measuring phosphate release kinetics in biological-systems. Proc Natl Acad Sci U S A 89(11):4884–4887
doi: 10.1073/pnas.89.11.4884
pubmed: 1534409
pmcid: 49192