Control of peptide deformylase activity by metal cations

Journal of Molecular Biology

Volumn 280, Issue 3, 1998, Pages 515-523

  Ragusa, Stéphane ^a   Blanquet, Sylvain ^a   Meinnel, Thierry ^a  

^a LABORATOIRE DE BIOCHIMIE   (France)

Author keywords

Activation; Activity; Metal ions; Nickel; Zinc

Indexed keywords

BACTERIAL ENZYME; BUFFER; CATION; METAL ION; METALLOPROTEIN; NICKEL; PEPTIDE; ZINC;

ARTICLE; ENZYME KINETICS; ESCHERICHIA COLI; GEOBACILLUS STEAROTHERMOPHILUS; NONHUMAN; PRIORITY JOURNAL; THERMUS THERMOPHILUS;

ESCHERICHIA COLI;

EID: 0032540979     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1998.1883     Document Type: Article

References (29)

1. Adams J.M. On the release of the formyl group from nascent protein. J. Mol. Biol. 33:1968;571-589
2. Ball L.A., Kaesberg P. Cleavage of the N-terminal formylmethionine residue from a bacteriophage coat protein in vitro. J. Mol. Biol. 79:1973;531-537
3. Ben-Bassat A., Bauer K., Chang S.-Y., Myambo K., Boosman A., Chang S. Processing of the initiation methionine from proteins properties of the Escherichia coli methionine aminopeptidase and its gene structure. J. Bacteriol. 169:1987;751-757
4. Bremer H., Dennis P.P. Modulation of chemical composition and other parameters of the cell by growth rate. Neidhardt F.C., Ingraham J.L., Low K.B., Magasanik B., Schaechter M., Umbarger H.E. Escherichia coli and Salmonella typhimurium Cellular and Molecular Biology. 1987;1527-1542 American Society for Microbiology, Washington, DC
5. Chang S.-Y.P., McGary E.C., Chang S. Methionine aminopeptidase gene of Escherichia coli is essential for cell growth. J. Bacteriol. 171:1989;4071-4072
6. Dardel F. MC-Fit Using Monte-Carlo methods to get accurate confidence limits on enzyme parameters. Comput. Appl. Biosci. 10:1994;273-275
7. Dardel F., Ragusa S., Lazennec C., Blanquet S., Meinnel T. Solution structure of nickel-peptide deformylase. J. Mol. Biol. 280:1998;501-513
8. Met formyltransferase severely impairs the growth of Escherichia coli. J. Bacteriol. 174:1992;4294-4301
9. Hausinger R.P. Biochemistry of Nickel. Frieden E. Biochemistry of the Elements. 1993;Plenum Publishing Corp, New-York
10. Hirel H. Spécificité de la méthionyl aminopeptidase. Thesis. 1990;Ecole Polytechnique, Palaiseau, France
11. Holland D.R., Hausrath A.C., Juers D., Matthews B.W. Structural analysis of zinc substitutions in the active site of thermolysin. Protein Sci. 4:1995;1955-1965
12. Housman D., Gillepsie D., Lodish H. Removal of formyl-methionine residue from nascent bacteriophage f2 protein. J. Mol. Biol. 65:1972;163-166
13. Lazennec C., Meinnel T. Formate dehydrogenase-coupled spectrophotometric assay of peptide deformylase. Anal. Biochem. 244:1997;180-182
14. Livingston D.M., Leder P. Deformylation and protein synthesis. Biochemistry. 8:1969;435-443
15. Mayaux J.-F., Blanquet S. Binding of zinc to Escherichia coli phenylalanyl transfer ribonucleic acid synthetase. Comparison with other aminoacyl transfer ribonucleic acid synthetases. Biochemistry. 20:1981;4647-4654
16. Mazel D., Pochet S., Marlière P. Genetic characterization of polypeptide deformylase, a distinctive enzyme of eubacterial translation. EMBO J. 13:1994;914-923
17. Met formyltransferase are encoded within the same operon in Escherichia coli. J. Bacteriol. 175:1993;7737-7740
18. Met formyltransferase. J. Bacteriol. 176:1994;7387-7390
19. Meinnel T., Blanquet S. Enzymatic properties of Escherichia coli peptide deformylase. J. Bacteriol. 177:1995;1883-1887
20. Meinnel T., Mechulam Y., Blanquet S. Methionine as translation start signal a review of the enzymes of the pathway in Escherichia coli. Biochimie (Paris). 75:1993;1061-1075
21. Meinnel T., Lazennec C., Blanquet S. Mapping of the active site zinc ligands of peptide deformylase. J. Mol. Biol. 254:1995;175-183
22. Meinnel T., Blanquet S., Dardel F. A new subclass of the zinc metalloproteases family revealed by the solution structure of peptide deformylase. J. Mol. Biol. 262:1996;375-386
23. Meinnel T., Lazennec C., Dardel F., Schmitter J.-M., Blanquet S. The C-terminal domain of peptide deformylase is disordered and dispensable for activity. FEBS Letters. 385:1996;91-95
24. Meinnel T., Lazennec C., Villoing S., Blanquet S. Structure-function relationships of the peptide deformylase family. Evidence for a common tertiary fold of the active site built around three conserved motifs and a metal ion. J. Mol. Biol. 267:1997;749-761
25. Moore S., Stein W.H. A modified ninhydrin reagent for the photometric determination of amino acids and related compounds. J. Biol. Chem. 211:1954;907-913
26. Pine M.J. Kinetics of maturation of the amino termini of the cell proteins of Escherichia coli. Biochim. Byophys. Acta. 174:1969;359-372
27. Rajagopalan P.T.R., Datta A., Pei D. Purification, characterization, and inhibition of peptide deformylase from Escherichia coli. Biochemistry. 36:1997;13910-13918
28. Rajagopalan P.T.R., Yu X.C., Pei D. Peptide deformylase a new type of mononuclear iron protein. J. Am. Chem. Soc. 119:1997;12418-12419
29. Veillon C., Vallee B.L. Atomic spectroscopy in metal analysis of enzymes and other biological material. Methods Enzymol. 54:1978;446-484