Characterization of full length and truncated type I human methionine aminopeptidases expressed from Escherichia coli

Biochemistry

Volumn 43, Issue 24, 2004, Pages 7892-7898

  Li, Jing Ya ^a   Chen, Ling Ling ^a   Cui, Yong Mei ^a   Luo, Qun Li ^a   Gu, Min ^a   Nan, Fa Jun ^a   Ye, Qi Zhuang ^a,b  

^a SHANGHAI INSTITUTE OF MATERIA MEDICA   (China)

^b UNIVERSITY OF KANSAS   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA; ESCHERICHIA COLI; FUNGUS RESISTANCE; HYDROLYSIS; PATHOLOGY; PHYSIOLOGY; POLYPEPTIDES; PROTEINS; TOXICITY; TUMORS;

ANTICANCER AGENTS; POTENT INHIBITION;

BIOCHEMISTRY;

ANTIINFECTIVE AGENT; ENZYME INHIBITOR; METHIONINE; METHIONYL AMINOPEPTIDASE; MUTANT PROTEIN; PEPTIDE DERIVATIVE; RECOMBINANT ENZYME; TETRAPEPTIDE; TRIPEPTIDE;

AMINO TERMINAL SEQUENCE; ARTICLE; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME INHIBITION; ENZYME SPECIFICITY; ENZYME SUBSTRATE; ESCHERICHIA COLI; HYDROLYSIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN PROCESSING; PROTEIN TARGETING; ZINC FINGER MOTIF;

AMINO ACID SEQUENCE; AMINOPEPTIDASES; BASE SEQUENCE; DNA PRIMERS; ENZYME ACTIVATION; ESCHERICHIA COLI; HYDROLYSIS; MOLECULAR SEQUENCE DATA; SEQUENCE HOMOLOGY, AMINO ACID;

ESCHERICHIA COLI; FUNGI; NEGIBACTERIA; PROKARYOTA;

EID: 2942750310     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0360859     Document Type: Article

References (29)

1. Bradshaw, R. A., Brickey, W. W., and Walker, K. W. (1998) N-terminal processing: the methionine aminopeptidase and N alpha-acetyl transferase families, Trends Biochem. Sci. 23, 263-267.
2. Tsunasawa, S., Stewart, J. W., and Sherman, F. (1985) Amino-terminal processing of mutant forms of yeast iso-1-cytochrome c, J. Biol. Chem. 260, 5382-5391.
3. Solbiati, J., Chapman-Smith, A., Miller, J. L., Miller, C. G., and Cronan, J. E. (1999) Processing of the N termini of nascent polypeptide chains requires deformylation prior to methionine removal, J. Mol. Biol. 290, 607-614.
4. Arfin, S. M., Kendall, R. L., Hall, L., Weaver, L. H., Stewart, A. E., Matthews, B. W., and Bradshaw, R. A. (1995) Eukaryotic methionyl aminopeptidases: two classes of cobalt-dependent enzymes, Proc. Natl. Acad. Sci. U.S.A. 92, 7714-7718.
5. Zuo, S., Guo, Q., Ling, C., and Chang, Y. H. (1995) Evidence that two zinc fingers in the methionine aminopeptidase from Saccharomyces cerevisiae are important for normal growth, Mol. Gen. Genet. 246, 247-253.
6. Chang, Y. H., Teichert, U., and Smith, J. A. (1992) Molecular cloning, sequencing, deletion, and overexpression of a methionine aminopeptidase gene from Saccharomyces cerevisiae, J. Biol. Chem. 267, 8007-8011.
7. Vetro, J. A., and Chang, Y. H. (2002) Yeast methionine aminopeptidase type 1 is ribosome-associated and requires its N-terminal zinc finger domain for normal function in vivo, J. Cell. Biol. 85, 678-688.
8. Chang, S. Y., McGary, E. C., and Chang, S. (1989) Methionine aminopeptidase gene of Escherichia coli is essential for cell growth, J. Bacteriol. 171, 4071-4072.
9. Miller, C. G., Kukral, A. M., Miller, J. L., and Movva, N. R. (1989) PepM is an essential gene in Salmonella typhimurium, J. Bacteriol. 171, 5215-5217.
10. Li, X., and Chang, Y. H. (1995) Amino-terminal protein processing in Saccharomyces cerevisiae is an essential function that requires two distinct methionine aminopeptidases, Proc. Natl. Acad. Sci. U.S.A. 92, 12357-12361.
11. Vaughan, M. D., Sampson, P. B., and Honek, J. F. (2002) Methionine in and out of proteins: targets for drug design, Curr. Med. Chem. 9, 385-409.
12. Perna, N. T., Plunkett, G., Burland, V., Mau, B., Glasner, J. D., Rose, D. J., Mayhew, G. F., Evans, P. S., Gregor, J., Kirkpatrick, H. A., Posfai, G., Hackett, J., Klink, S., Boutin, A., Shao, Y., Miller, L., Grotbeck, E. J., Davis, N. W., Lim, A., Dimalanta, E. T., Potamousis, K. D., Apodaca, J., Anantharaman, T. S., Lin, J., Yen, G., Schwartz, D. C., Welch, R. A., and Blattner, F. R. (2001) Genome sequence of enterohaemorrhagic Escherichia coli O157: H7. Nature 409, 529-533.
13. Guan, K. L., and Dixon, J. E. (1991) Eukaryotic proteins expressed in Escherichia coli: an improved thrombin cleavage and purification procedure of fusion proteins with glutathione S-transferase, Anal. Biochem. 192, 262-267.
14. Zhou, Y., Guo, X. C., Yi, T., Yoshimoto, T., and Pei, D. H. (2000) Two continuous spectrophotometric assays for methionine amino-peptidase, Anal. Biochem. 280, 159-165.
15. Luo, Q. L., Li, J. Y., Liu, Z. Y., Chen, L. L., Li, J., Qian, Z., Shen, Q., Li, Y., Lushington, G. H., Ye, Q. Z., and Nan, F. J. (2003) Discovery and structural modification of inhibitors of methionine aminopeptidases from Escherichia coli and Saccharomyces cerevisiae, J. Med. Chem. 46, 2631-2640.
16. Turk, B. E., Griffith, E. C., Wolf, S., Biemann, K., Chang, Y. H., Liu, J. O. (1999) Selective inhibition of amino-terminal methionine processing by TNP-470 and ovalicin in endothelial cells, Chem. Biol. 6, 823-833.
17. Dummitt, B., Fei, Y., and Chang, Y. H. (2002) Functional expression of human methionine aminopeptidase type I in Saccharomyces cerevisiae, Protein Pept. Lett. 9, 295-303.
18. Yang, G., Kirkpatrick, R. B., Ho, T., Zhang, G. F., Liang, P. H., Johanson, K. O., Casper, D. J., Doyle, M. L., Marino, J. P., Thompson, S. K., Chen, W., Tew, D. G., and Meek, T. D. (2001) Steady-state kinetic characterization of substrates and metal ion specificities of the full-length and N-terminally truncated recombinant human methionine aminopeptidases (type 2), Biochemistry 40, 10645-10654.
19. Li, J. Y., Chen, L. L., Cui, Y. M., Luo, Q. L., Li, J., Nan, F. J., and Ye, Q. Z. (2003) Specificity for inhibitors of metal-substituted methionine aminopeptidase, Biochem. Biophys. Res. Commun. 307, 172-179.
20. D'souza, V. M., and Holz, R. C. (1999) The methionyl aminopeptidase from Escherichia coli can function as an iron(II) enzyme, Biochemistry 38, 11079-11085.
21. Walker, K. W., Yi, E., and Bradshaw, R. A. (1999) Yeast (Saccharomyces cerevisiae) methionine aminopeptidase I: rapid purification and improved activity assay, Biotechnol. Appl. Biochem. 29, 157-163.
22. Sin, N., Meng, L., Wang, M. Q., Wen, J. J., Bornmann, W. G., and Crews, C. W. (1997) The antiangiogenic agent fumagillin covalently binds and inhibits the methionine aminopeptidase 2, Proc. Natl. Acad. Sci. U.S.A. 94, 6099-6103.
23. Griffith, E. C., Su, Z., Niwayama, S., Ramsay, C. A., Chang, Y. H., and Liu, J. O. (1998) Molecular recognition of angiogenesis inhibitors fumagillin and ovalicin by methionine aminopeptidase 2, Proc. Natl. Acad. Sci. U.S.A. 95, 15183-15188.
24. Towbin, H., Bair, K. W., DeCaprio, J. A., Eck, M., Kim, S., Kinder, F. R., Morollo, A., Mueller, D. R., Schindler, P., Song, H. K., Oostrum, J., Versace, R. W., Voshol, J., Wood, J., Zabludoff, S., and Phillips, P. E. (2003) Proteomics based target identification: Bengamides as a new class of methionine amino-peptidase inhibitors, J. Biol. Chem. 278, 52964-52971.
25. Keding, S. J., Dales, N. A., Lim, S., Beauliu, D., and Rich, D. H. (1998) Synthesis of (3R)-amino-(2S)-hydroxy amino acids for inhibition of methionine aminopeptidase-1, Synth. Commun. 28, 4463-4470.
26. Lowther, W. T., Zhang, Y., Sampson, P. B., Honek, J. F., and Matthews, B. W. (1999) Insights into the mechanism of Escherichia coli methionine aminopeptidase from the structural analysis of reaction products and phosphorus-based transition-state analogues, Biochemistry 38, 14810-14819.
27. Lowther, W. T., and Matthews, B. W. (2000) Structure and function of the methionine aminopeptidases, Biochim. Biophys. Acta 1477, 157-167.
28. Li, J. Y., Cui, Y. M., Chen, L. L., Gu, M., Li, J., Nan, F. J., and Ye, Q. Z. (2004) Mutations at the S1 site of methionine aminopeptidases from Escherichia coli and Homosapiens reveal the residues critical for substrate specificity, J. Biol. Chem. 279, 21128-21134.
29. Liu, S., Widom, J., Kemp, C. W., Crews, C. M., and Clardy, J. (1998) Structure of human methionine aminopeptidase-2 complexed with fumagillin, Science 282, 1324-1327.