Mycobacterium tuberculosis Rv1916 is an Acetyl-CoA-Binding Protein.
Mycobacterium tuberculosis
Rv1916
acyl-CoA-binding protein
glyoxylate shunt
isocitrate lyase
Journal
Chembiochem : a European journal of chemical biology
ISSN: 1439-7633
Titre abrégé: Chembiochem
Pays: Germany
ID NLM: 100937360
Informations de publication
Date de publication:
17 07 2023
17 07 2023
Historique:
revised:
15
05
2023
received:
27
02
2023
medline:
18
7
2023
pubmed:
22
5
2023
entrez:
21
5
2023
Statut:
ppublish
Résumé
Isocitrate lyase (ICL) isoform 2 is an essential enzyme for some clinical Mycobacterium tuberculosis (Mtb) strains during infection. In the laboratory Mtb strain H37Rv, the icl2 gene encodes two distinct gene products - Rv1915 and Rv1916 - due to a frameshift mutation. This study aims to characterise these two gene products to understand their structure and function. While we were unable to produce Rv1915 recombinantly, soluble Rv1916 was obtained with sufficient yield for characterisation. Kinetic studies using UV-visible spectrophotometry and
Identifiants
pubmed: 37211532
doi: 10.1002/cbic.202300162
doi:
Substances chimiques
Acetyl Coenzyme A
72-89-9
Isocitrate Lyase
EC 4.1.3.1
Bacterial Proteins
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
e202300162Informations de copyright
© 2023 The Authors. ChemBioChem published by Wiley-VCH GmbH.
Références
J. E. Gomez, J. D. McKinney, Tuberculosis 2004, 84, 29-44.
L. P. S. de Carvalho, S. M. Fischer, J. Marrero, C. Nathan, S. Ehrt, K. Y. Rhee, Chem. Biol. 2010, 17, 1122-1131.
S. K. Dolan, M. Welch, Annu. Rev. Microbiol. 2018, 72, 309-330.
K. Borah, T. A. Mendum, N. D. Hawkins, J. L. Ward, M. H. Beale, G. Larrouy-Maumus, A. Bhatt, M. Moulin, M. Haertlein, G. Strohmeier, H. Pichler, V. T. Forsyth, S. Noack, C. W. Goulding, J. McFadden, D. J. V. Beste, Mol. Syst. Biol. 2021, 17, e10280.
K. Höner Zu Bentrup, A. Miczak, D. L. Swenson, D. G. Russell, J. Bacteriol. 1999, 181, 7161-7167.
J. Bi, Y. Wang, H. Yu, X. Qian, H. Wang, J. Liu, X. Zhang, Sci. Rep. 2017, 7, 44826.
L. Xie, X. Wang, J. Zeng, M. Zhou, X. Duan, Q. Li, Z. Zhang, H. Luo, L. Pang, W. Li, G. Liao, X. Yu, Y. Li, H. Huang, J. Xie, Int. J. Biochem. Cell Biol. 2015, 59, 193-202.
M. Zhou, L. Xie, Z. Yang, J. Zhou, J. Xie, J. Biomol. Struct. Dyn. 2017, 35, 1030-1041.
L. Xie, W. Liu, Q. Li, S. Chen, M. Xu, Q. Huang, J. Zeng, M. Zhou, J. Xie, J. Proteome Res. 2015, 14, 107-119.
B. X. C. Kwai, A. J. Collins, M. J. Middleditch, J. Sperry, G. Bashiri, I. K. H. Leung, RSC Med. Chem. 2021, 12, 57-61.
R. P. Bhusal, W. Jiao, B. X. C. Kwai, J. Reynisson, A. J. Collins, J. Sperry, G. Bashiri, I. K. H. Leung, Nat. Commun. 2019, 10, 4639.
M. M. Moynihan, A. S. Murkin, Biochemistry 2014, 53, 178-187.
A. Rehman, B. A. McFadden, Curr. Microbiol. 1997, 35, 267-269.
R. D. Fleischmann, D. Alland, J. A. Eisen, L. Carpenter, O. White, J. Peterson, R. DeBoy, R. Dodson, M. Gwinn, D. Haft, E. Hickey, J. F. Kolonay, W. C. Nelson, L. A. Umayam, M. Ermolaeva, S. L. Salzberg, A. Delcher, T. Utterback, J. Weidman, H. Khouri, J. Gill, A. Mikula, W. Bishai, W. R. Jacobs Jr, J. C. Venter, C. M. Fraser, J. Bacteriol. 2002, 184, 5479-5490.
M. Antil, S. G. Gouin, V. Gupta, Front. Bioeng. Biotechnol 2020, 8, 522.
M. Antil, J. Sharma, Y. Brissonnet, M. Choudhary, S. Gouin, V. Gupta, Int. J. Biol. Macromol. 2019, 141, 927-936.
M. Antil, V. Gupta, Biochim. Biophys. Acta 2022, 1866, 130130.
R. Chen, Biotechnol. Adv. 2012, 30, 1102-1107.
A. J. Miles, R. W. Janes, B. A. Wallace, Chem. Soc. Rev. 2021, 50, 8400-8413.
H. Tegel, S. Tourle, J. Ottosson, A. Persson, Prot. Exp. Purif. 2010, 69, 159-167.
L. Belval, A. Marquette, P. Mestre, M.-C. Piron, G. Demangeat, D. Merdinoglu, J.-F. Chich, Prot. Exp. Purif. 2015, 109, 29-34.
E. De Bernardez Clark, Curr. Opin. Biotechnol. 1998, 9, 157-163.
H. Yamaguchi, M. Miyazaki, Biomolecules 2014, 4, 235-251.
G. H. Dixon, H. L. Kornberg, Biochem. J. 1959, 72, 3P.
R. P. Bhusal, K. Patel, B. X. C. Kwai, A. Swartjes, G. Bashiri, J. Reynisson, J. Sperry, I. K. H. Leung, MedChemComm 2017, 8, 2155-2163.
C. Dalvit, P. Pevarello, M. Tatò, M. Veronesi, A. Vulpetti, M. Sundström, J. Biomol. NMR 2000, 18, 65-68.
C. Dalvit, G. Fogliatto, A. Stewart, M. Veronesi, B. Stockman, J. Biomol. NMR 2001, 21, 349-359.
R. Huang, I. K. H. Leung, In Methods in Enzymology, Vol. 615 (Ed: A. J. Wand), Elsevier, 2019, Ch. 14, 477-500.
Z. S. Derewenda, Methods 2004, 34, 354-363.
E. J. Muñoz-Elías, J. D. McKinney, Nat. Med. 2005, 11, 638-644.
Y. Tanaka, T. Yoshida, K. Watanabe, Y. Izumi, T. Mitsunaga, Eur. J. Biochem. 1997, 249, 820-825.
G. K. H. Siu, W. C. Yam, Y. Zhang, R. Y. T. Kao, Antimicrob. Agents Chemother. 2014, 58, 6093-6100.
P. S. C. Wu, G. Otting, J. Magn. Reson. 2005, 176, 115-119.
C. Roumestand, D. Canet, J. Magn. Reson. 2000, 147, 331-339.
T. M. McPhillips, S. E. McPhillips, H. J. Chiu, A. E. Cohen, A. M. Deacon, P. J. Ellis, E. Garman, A. Gonzalez, N. K. Sauter, R. P. Phizackerley, S. M. Soltis, P. Kuhn, J. Synchrotron Radiat. 2022, 9 (Pt6), 401-406.
W. Kabsch, Acta Crystallogr. Sect. D 2010, 66, 133-144.
P. R. Evans, G. N. Murshudov, Acta Crystallogr. Sect. D: Biol. Crystallogr. 2013, 69, 1204-1214.
A. J. McCoy, R. W. Grosse-Kunstleve, P. D. Adams, M. D. Winn, L. C. Storoni, R. J. Read, J. Appl. Crystallogr. 2007, 40, 658-674.
P. Emsley, K. Cowtan, Acta Crystallogr. Sect. D 2004, 60, 2126-2132.
G. N. Murshudov, P. Skubák, A. A. Lebedev, N. S. Pannu, R. A. Steiner, R. A. Nicholls, M. D. Winn, F. Long, A. A. Vagin, Acta Crystallogr. Sect. D: Biol. Crystallogr. 2011, 67, 355-367.
R. P. Joosten, F. Long, G. N. Murshudov, A. Perrakisa, IUCrJ 2014, 1, 213-220.
I. W. Davis, A. Leaver-Fay, V. B. Chen, J. N. Block, G. J. Kapral, X. Wang, L. W. Murray, W. B. III Arendall, J. Snoeyink, J. S. Richardson, D. C. Richardson, Nucleic Acids Res. 2007, 35 (suppl_2), W375-W383.
M. S. Weiss, J. Appl. Crystallogr. 2001, 34, 130-135.
K. Diederichs, P. A. Karplus, Acta Crystallogr. Sect. D: Struct. Biol. 2013, 69, 1215-1222.