Methionine Aminopeptidases from Mycobacterium tuberculosis as Novel Antimycobacterial Targets

Chemistry and Biology

Volumn 17, Issue 1, 2010, Pages 86-97

  Olaleye, Omonike ^a,b   Raghunand, Tirumalai R ^a   Bhat, Shridhar ^a   He, Jian ^a   Tyagi, Sandeep ^a   Lamichhane, Gyanu ^a   Gu, Peihua ^c   Zhou, Jiangbing ^c   Zhang, Ying ^c   Grosset, Jacques ^a   Bishai, William R ^a   Liu, Jun O ^a  

^a JOHNS HOPKINS UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b TEXAS SOUTHERN UNIVERSITY   (United States)

^c JOHNS HOPKINS BLOOMBERG SCHOOL OF PUBLIC HEALTH   (United States)

Author keywords

CHEMBIO; HUMDISEASE; MICROBIO

Indexed keywords

AMINOPEPTIDASE; METHIONYL AMINOPEPTIDASE; TUBERCULOSTATIC AGENT;

AMINO ACID SEQUENCE; ANTIBIOTIC RESISTANCE; ARTICLE; CHEMISTRY; DRUG ANTAGONISM; ENZYMOLOGY; GENE EXPRESSION REGULATION; GENETICS; GROWTH, DEVELOPMENT AND AGING; HUMAN; METABOLISM; MICROBIOLOGICAL EXAMINATION; MOLECULAR GENETICS; MYCOBACTERIUM TUBERCULOSIS; SEQUENCE ALIGNMENT; TUBERCULOSIS;

AMINO ACID SEQUENCE; AMINOPEPTIDASES; ANTITUBERCULAR AGENTS; DRUG RESISTANCE, BACTERIAL; GENE EXPRESSION REGULATION, BACTERIAL; HUMANS; MICROBIAL SENSITIVITY TESTS; MOLECULAR SEQUENCE DATA; MYCOBACTERIUM TUBERCULOSIS; SEQUENCE ALIGNMENT; TUBERCULOSIS;

BACTERIA (MICROORGANISMS); MYCOBACTERIUM TUBERCULOSIS;

EID: 75149115775     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.chembiol.2009.12.014     Document Type: Article

References (30)

1. Addlagatta A., Hu X., Liu J.O., and Matthews B.W. Structural basis for the functional differences between type I and type II human methionine aminopeptidases. Biochemistry 44 (2005) 14741-14749
2. Addlagatta A., Quillin M.L., Omotoso O., Liu J.O., and Matthews B.W. Identification of an SH3-binding motif in a new class of methionine aminopeptidases from Mycobacterium tuberculosis suggests a mode of interaction with the ribosome. Biochemistry 44 (2005) 7166-7174
3. Arfin S.M., Kendall R.L., Hall L., Weaver L.H., Stewart A.E., Matthews B.W., and Bradshaw R.A. Eukaryotic methionyl aminopeptidases: two classes of cobalt-dependent enzymes. Proc. Natl. Acad. Sci. USA 92 (1995) 7714-7718
4. Bernier S.G., Taghizadeh N., Thompson C.D., Westlin W.F., and Hannig G. Methionine aminopeptidases type I and type II are essential to control cell proliferation. J. Cell. Biochem. 95 (2005) 1191-1203
5. Boxem M., Tsai C.W., Zhang Y., Saito R.M., and Liu J.O. The C. elegans methionine aminopeptidase 2 analog map-2 is required for germ cell proliferation. FEBS Lett. 576 (2004) 245-250
6. Byrne S.T., Gu P., Zhou J., Denkin S.M., Chong C., Sullivan D., Liu J.O., and Zhang Y. Pyrrolidine dithiocarbamate and diethyldithiocarbamate are active against growing and nongrowing persister Mycobacterium tuberculosis. Antimicrob. Agents Chemother. 51 (2007) 4495-4497
7. Chang S.Y., McGary E.C., and Chang S. Methionine aminopeptidase gene of Escherichia coli is essential for cell growth. J. Bacteriol. 171 (1989) 4071-4072
8. Chang Y.H., Teichert U., and Smith J.A. Molecular cloning, sequencing, deletion, and overexpression of a methionine aminopeptidase gene from Saccharomyces cerevisiae. J. Biol. Chem. 267 (1992) 8007-8011
9. Chen X., Chong C.R., Shi L., Yoshimoto T., Sullivan Jr. D.J., and Liu J.O. Inhibitors of Plasmodium falciparum methionine aminopeptidase 1b possess antimalarial activity. Proc. Natl. Acad. Sci. USA 103 (2006) 14548-14553
10. Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C., Harris D., Gordon S.V., Eiglmeier K., Gas S., Barry III C.E., et al. Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. Nature 393 (1998) 537-544
11. Dye C. Global epidemiology of tuberculosis. Lancet 367 (2006) 938-940
12. Fauci A.S. Multidrug-resistant and extensively drug-resistant tuberculosis: the National Institute of Allergy and Infectious Diseases Research agenda and recommendations for priority research. J. Infect. Dis. 197 (2008) 1493-1498
13. Gandhi N.R., Moll A., Sturm A.W., Pawinski R., Govender T., Lalloo U., Zeller K., Andrews J., and Friedland G. Extensively drug-resistant tuberculosis as a cause of death in patients co-infected with tuberculosis and HIV in a rural area of South Africa. Lancet 368 (2006) 1575-1580
14. Giglione C., Vallon O., and Meinnel T. Control of protein life-span by N-terminal methionine excision. EMBO J. 22 (2003) 13-23
15. Griffith E.C., Su Z., Turk B.E., Chen S., Chang Y.-W., Wu Z., Biemann K., and Liu J.O. Methionine aminopeptidase (type 2) is the common target for angiogenesis inhibitors AGM-1470 and ovalicin. Chem. Biol. 4 (1997) 461-471
16. Hu X., Addlagatta A., Lu J., Matthews B.W., and Liu J.O. Elucidation of the function of type 1 human methionine aminopeptidase during cell cycle progression. Proc. Natl. Acad. Sci. USA 103 (2006) 18148-18153
17. Li X., and Chang Y.H. Amino-terminal protein processing in Saccharomyces cerevisiae is an essential function that requires two distinct methionine aminopeptidases. Proc. Natl. Acad. Sci. USA 92 (1995) 12357-12361
18. Lowther W.T., and Matthews B.W. Structure and function of the methionine aminopeptidases. Biochim. Biophys. Acta 1477 (2000) 157-167
19. Miller C.G., Kukral A.M., Miller J.L., and Movva N.R. pepM is an essential gene in Salmonella typhimurium. J. Bacteriol. 171 (1989) 5215-5217
20. Narayanan S.S., Ramanujan A., Krishna S., and Nampoothiri K.M. Purification and biochemical characterization of methionine aminopeptidase (MetAP) from Mycobacterium smegmatis mc2155. Appl. Biochem. Biotechnol. 151 (2008) 512-521
21. Raghunand T.R., Bishai W.R., and Chen P. Towards establishing a method to screen for inhibitors of essential genes in mycobacteria: evaluation of the acetamidase promoter. Int. J. Antimicrob. Agents 28 (2006) 36-41
22. Raviglione M.C. The TB epidemic from 1992 to 2002. Tuberculosis (Edinb.) 83 (2003) 4-14
23. Ribeiro-Guimaraes M.L., and Pessolani M.C. Comparative genomics of mycobacterial proteases. Microb. Pathog. 43 (2007) 173-178
24. Sin N., Meng L., Wang M.Q., Wen J.J., Bornmann W.G., and Crews C.M. The anti-angiogenic agent fumagillin covalently binds and inhibits the methionine aminopeptidase, MetAP-2. Proc. Natl. Acad. Sci. USA 94 (1997) 6099-6103
25. Solbiati J., Chapman-Smith A., Miller J.L., Miller C.G., and Cronan Jr. J.E. Processing of the N termini of nascent polypeptide chains requires deformylation prior to methionine removal. J. Mol. Biol. 290 (1999) 607-614
26. Yeh J.R., Ju R., Brdlik C.M., Zhang W., Zhang Y., Matyskiela M.E., Shotwell J.D., and Crews C.M. Targeted gene disruption of methionine aminopeptidase 2 results in an embryonic gastrulation defect and endothelial cell growth arrest. Proc. Natl. Acad. Sci. USA 103 (2006) 10379-10384
27. Zhang Y. The magic bullets and tuberculosis drug targets. Annu. Rev. Pharmacol. Toxicol. 45 (2005) 529-564
28. Zhang X., Chen S., Hu Z., Zhang L., and Wang H. Expression and characterization of two functional methionine aminopeptidases from Mycobacterium tuberculosis H37Rv. Curr. Microbiol. 59 (2009) 520-525
29. Zhou Y., Guo X.C., Yi T., Yoshimoto T., and Pei D. Two continuous spectrophotometric assays for methionine aminopeptidase. Anal. Biochem. 280 (2000) 159-165
30. Zignol M., Hosseini M.S., Wright A., Weezenbeek C.L., Nunn P., Watt C.J., Williams B.G., and Dye C. Global incidence of multidrug-resistant tuberculosis. J. Infect. Dis. 194 (2006) 479-485