Structure and functional regulation of RipA, a mycobacterial enzyme essential for daughter cell separation

Structure

Volumn 18, Issue 9, 2010, Pages 1184-1190

  Ruggiero, Alessia ^a   Marasco, Daniela ^a,b   Squeglia, Flavia ^a,b   Soldini, Silvia ^c   Pedone, Emilia ^a   Pedone, Carlo ^b   Berisio, Rita ^a  

^a CNR   (Italy)

^b UNIVERSITY OF NAPLES FEDERICO II   (Italy)

^c CATHOLIC UNIVERSITY   (Italy)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; ENZYME PRECURSOR; PROTEINASE;

ARTICLE; BACTERIAL CELL WALL; CELL DIVISION; CELL SEPARATION; DAUGHTER CELL; ENZYME ACTIVITY; ENZYME STRUCTURE; MOLECULAR CLONING; MYCOBACTERIUM TUBERCULOSIS; NONHUMAN; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN CLEAVAGE; PROTEIN DEGRADATION; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN PURIFICATION;

AMINO ACID SEQUENCE; BACTERIAL PROTEINS; CELL DIVISION; CELL WALL; ENDOPEPTIDASES; HYDROLYSIS; MODELS, GENETIC; MOLECULAR SEQUENCE DATA; MYCOBACTERIUM TUBERCULOSIS; PROTEIN STRUCTURE, TERTIARY; STRUCTURE-ACTIVITY RELATIONSHIP;

BACTERIA (MICROORGANISMS); MYCOBACTERIUM TUBERCULOSIS;

EID: 77956331325     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.str.2010.06.007     Document Type: Article

References (35)

1. Aramini J.M., Rossi P., Huang Y.J., Zhao L., Jiang M., Maglaqui M., Xiao R., Locke J., Nair R., Rost B., et al. Solution NMR structure of the NlpC/P60 domain of lipoprotein Spr from Escherichia coli: structural evidence for a novel cysteine peptidase catalytic triad. Biochemistry 2008, 47:9715-9717.
2. Bateman A., Rawlings N.D. The CHAP domain: a large family of amidases including GSP amidase and peptidoglycan hydrolases. Trends Biochem. Sci. 2003, 28:234-237.
3. Downing K.J., Mischenko V.V., Shleeva M.O., Young D.I., Young M., Kaprelyants A.S., Apt A.S., Mizrahi V. Mutants of Mycobacterium tuberculosis lacking three of the five rpf-like genes are defective for growth in vivo and for resuscitation in vitro. Infect. Immun. 2005, 73:3038-3043.
4. Engh R.A., Huber R. Accurate bond and angle parameters for X-ray protein structure refinement. Acta Crystallogr. A 1991, 47:392-400.
5. Fukushima T., Kitajima T., Yamaguchi H., Ouyang Q., Furuhata K., Yamamoto H., Shida T., Sekiguchi J. Identification and characterization of novel cell wall hydrolase CwlT: a two-domain autolysin exhibiting n-acetylmuramidase and DL-endopeptidase activities. J. Biol. Chem. 2008, 283:11117-11125.
6. Hett E.C., Rubin E.J. Bacterial growth and cell division: a mycobacterial perspective. Microbiol. Mol. Biol. Rev. 2008, 72:126-156.
7. Hett E.C., Chao M.C., Steyn A.J., Fortune S.M., Deng L.L., Rubin E.J. A partner for the resuscitation-promoting factors of Mycobacterium tuberculosis. Mol. Microbiol. 2007, 66:658-668.
8. Hett E.C., Chao M.C., Deng L.L., Rubin E.J. A mycobacterial enzyme essential for cell division synergizes with resuscitation-promoting factor. PLoS Pathog. 2008, 4.
9. Kana B.D., Mizrahi V. Resuscitation-promoting factors as lytic enzymes for bacterial growth and signaling. FEMS Immunol. Med. Microbiol. 2010, 58:39-50.
10. Kana B.D., Gordhan B.G., Downing K.J., Sung N., Vostroktunova G., Machowski E.E., Tsenova L., Young M., Kaprelyants A., Kaplan G., Mizrahi V. The resuscitation-promoting factors of Mycobacterium tuberculosis are required for virulence and resuscitation from dormancy but are collectively dispensable for growth in vitro. Mol. Microbiol. 2008, 67:672-684.
11. Kaufmann S.H. Tuberculosis: Deadly combination. Nature 2008, 453:295-296.
12. Langer G., Cohen S.X., Lamzin V.S., Perrakis A. Automated macromolecular model building for X-ray crystallography using ARP/wARP version 7. Nat. Protoc. 2008, 3:1171-1179.
13. Laskowski R.A., Rullmannn J.A., MacArthur M.W., Kaptein R., Thornton J.M. AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR. J. Biomol. NMR 1996, 8:477-486.
14. Layec S., Decaris B., Leblond-Bourget N. Diversity of Firmicutes peptidoglycan hydrolases and specificities of those involved in daughter cell separation. Res. Microbiol. 2008, 159:507-515.
15. Layec S., Gerard J., Legue V., Chapot-Chartier M.P., Courtin P., Borges F., Decaris B., Leblond-Bourget N. The CHAP domain of Cse functions as an endopeptidase that acts at mature septa to promote Streptococcus thermophilus cell separation. Mol. Microbiol. 2009, 71:1205-1217.
16. Menard R., Carmona E., Takebe S., Dufour E., Plouffe C., Mason P., Mort J.S. Autocatalytic processing of recombinant human procathepsin L. Contribution of both intermolecular and unimolecular events in the processing of procathepsin L in vitro. J. Biol. Chem. 1998, 273:4478-4484.
17. Mukamolova G.V., Kaprelyants A.S., Young D.I., Young M., Kell D.B. A bacterial cytokine. Proc. Natl. Acad. Sci. USA 1998, 95:8916-8921.
18. Mukamolova G.V., Turapov O.A., Young D.I., Kaprelyants A.S., Kell D.B., Young M. A family of autocrine growth factors in Mycobacterium tuberculosis. Mol. Microbiol. 2002, 46:623-635.
19. Murshudov G.N., Vagin A.A., Dodson E.J. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr. D Biol. Crystallogr. 1997, 53:240-255.
20. Otwinowski Z., Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 1997, 276:307-326.
21. Potterton E., Briggs P., Turkenburg M., Dodson E. A graphical user interface to the CCP4 program suite. Acta Crystallogr. D Biol. Crystallogr. 2003, 59:1131-1137.
22. Rossi P., Aramini J.M., Xiao R., Chen C.X., Nwosu C., Owens L.A., Maglaqui M., Nair R., Fischer M., Acton T.B., et al. Structural elucidation of the Cys-His-Glu-Asn proteolytic relay in the secreted CHAP domain enzyme from the human pathogen Staphylococcus saprophyticus. Proteins 2009, 74:515-519.
23. Rozman J., Stojan J., Kuhelj R., Turk V., Turk B. Autocatalytic processing of recombinant human procathepsin B is a bimolecular process. FEBS Lett. 1999, 459:358-362.
24. ΔDUFRpfB from M. tuberculosis. J. Mol. Biol. 2009, 385:153-162.
25. Ruggiero A., Squeglia F., Esposito C., Marasco D., Pedone E., Pedone C., Berisio R. Expression, purification, crystallization and preliminary X-ray crystallographic analysis of the resuscitation promoting factor interacting protein RipA from M. tuberculosis. Protein Pept. Lett. 2010, 17:70-73.
26. Schroder K., Tschopp J. The inflammasomes. Cell 2010, 140:821-832.
27. Shah I.M., Dworkin J. Induction and regulation of a secreted peptidoglycan hydrolase by a membrane Ser/Thr kinase that detects muropeptides. Mol. Microbiol 2010.
28. Shah I.M., Laaberki M.H., Popham D.L., Dworkin J. A eukaryotic-like Ser/Thr kinase signals bacteria to exit dormancy in response to peptidoglycan fragments. Cell 2008, 135:486-496.
29. Sheldrick G.M. A short history of SHELX. Acta Crystallogr. A 2008, 64:112-122.
30. Sripa J., Laha T., To J., Brindley P.J., Sripa B., Kaewkes S., Dalton J.P., Robinson M.W. Secreted cysteine proteases of the carcinogenic liver fluke, Opisthorchis viverrini: regulation of cathepsin F activation by autocatalysis and trans-processing by cathepsin B. Cell Microbiol. 2010, 12:781-795.
31. Telkov M.V., Demina G.R., Voloshin S.A., Salina E.G., Dudik T.V., Stekhanova T.N., Mukamolova G.V., Kazaryan K.A., Goncharenko A.V., Young M., Kaprelyants A.S. Proteins of the Rpf (resuscitation promoting factor) family are peptidoglycan hydrolases. Biochemistry (Mosc.) 2006, 71:414-422.
32. Terwilliger T. SOLVE and RESOLVE: automated structure solution, density modification and model building. J. Synchrotron Radiat. 2004, 11:49-52.
33. Tufariello J.M., Mi K., Xu J., Manabe Y.C., Kesavan A.K., Drumm J., Tanaka K., Jacobs W.R., Chan J. Deletion of the Mycobacterium tuberculosis resuscitation-promoting factor Rv1009 gene results in delayed reactivation from chronic tuberculosis. Infect. Immun. 2006, 74:2985-2995.
34. Warner D.F., Mizrahi V. The survival kit of Mycobacterium tuberculosis. Nat. Med. 2007, 13:282-284.
35. Wittlin S., Rosel J., Hofmann F., Stover D.R. Mechanisms and kinetics of procathepsin D activation. Eur. J. Biochem. 1999, 265:384-393.