A novel serralysin metalloprotease from Deinococcus radiodurans

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1784, Issue 9, 2008, Pages 1256-1264

  Basu, Bhakti ^a   Apte, Shree Kumar ^a  

^a BHABHA ATOMIC RESEARCH CENTRE   (India)

Author keywords

Deinococcus; Serralysin like extracellular metalloprotease; Zn +2 Ca+2 dependency

Indexed keywords

CALCIUM; METALLOPROTEINASE; METHIONINE; PROTEIN; SERRALYSIN; THROMBOSPONDIN; THROMBOSPONDIN 3; UNCLASSIFIED DRUG; ZINC; ZINC BINDING PROTEIN; BACTERIAL DNA; BACTERIAL PROTEIN; RECOMBINANT PROTEIN;

AMINO ACID SUBSTITUTION; AMINO TERMINAL SEQUENCE; ARTICLE; CALCIUM BINDING; DEINOCOCCUS RADIODURANS; DELETION MUTANT; ENZYME RELEASE; GENE EXPRESSION; GENETIC CONSERVATION; GRAM NEGATIVE BACTERIUM; GRAM POSITIVE BACTERIUM; NONHUMAN; NUCLEOTIDE SEQUENCE; OPEN READING FRAME; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DETERMINATION; PROTEIN DOMAIN; PROTEIN FAMILY; RADIOSENSITIVITY; AMINO ACID SEQUENCE; BINDING SITE; BIOLOGY; CHEMISTRY; DEINOCOCCUS; ENZYMOLOGY; GENE DELETION; GENETICS; MASS SPECTROMETRY; METABOLISM; MOLECULAR GENETICS; MUTAGENESIS; PHYLOGENY; SEQUENCE HOMOLOGY;

DEINOCOCCUS; DEINOCOCCUS RADIODURANS; EUKARYOTA; NEGIBACTERIA; POSIBACTERIA;

AMINO ACID SEQUENCE; BACTERIAL PROTEINS; BASE SEQUENCE; BINDING SITES; CALCIUM; COMPUTATIONAL BIOLOGY; CONSERVED SEQUENCE; DEINOCOCCUS; DNA, BACTERIAL; METALLOENDOPEPTIDASES; MOLECULAR SEQUENCE DATA; MUTAGENESIS; PHYLOGENY; RECOMBINANT PROTEINS; SEQUENCE DELETION; SEQUENCE HOMOLOGY, AMINO ACID; SPECTROMETRY, MASS, MATRIX-ASSISTED LASER DESORPTION-IONIZATION; ZINC;

EID: 53149131763     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2008.05.009     Document Type: Article

References (37)

1. C.C. Häse, R.A. Finkelstein, Bacterial extracellular zinc-containing metalloproteases, Microbiol. Mol. Biol. Rev. 57 (1993) 823-837.
2. N.D. Rawlings, A.J. Barrett, Evolutionary families of metallopeptidases, Methods Enzymol. 248 (1997) 183-228.
3. H. Maeda, K. Morihara, Serralysin and related bacterial proteinases, Methods Enzymol. 248 (1995) 395-413.
4. W. Bode, F.X. Gomis-Rüth, W. Stöcker, Astacins, serralysins, snake venomand matrix metalloproteinases exhibit identical zinc-binding environments (HEXXHXXGXXH and Met-turn) and topologies and should be grouped into a common family, the metzincins"metzincins", FEBS Lett. 331 (1993) 134-140.
5. W. Stocker, F. Grams, U. Baumann, P. Reinemer, F.X. Gomis-Ruth, D.B. Mckay, W. Bode, The metzincins - Topological and sequential relations between the astacins, adamalysins, serralysins, and matrixins (collagenases) define a superfamily of zinc-peptidases, Protein Sci. 4 (1995) 823-840.
6. F.X. Gomis-Ruth, Structural aspects of the metzincin clan of metalloendopeptidases, Mol. Biotechnol. 24 (2003) 157-202.
7. P. Delepelaire, C. Wandersman, Protein secretion in gram-negative bacteria. The extracellular metalloprotease B from Erwinia chrysanthemi contains a C-terminal secretion signal analogous to that of Escherichia coli alpha-hemolysin, J. Biol. Chem. 265 (1990) 17118-17125.
8. H.E. Van Wart, H. Birkedal-Hansen, The cysteine switch: a principle of regulation of metalloproteinase activity with potential applicability to the entire matrix metalloproteinase gene family, Proc. Natl. Acad. Sci. U. S. A. 87 (1990) 5578-5582.
9. G.S. Dahler, F. Barras, N.T. Keen, Cloning of genes encoding extracellular metalloproteases from Erwinia chrysanthemi EC16, J. Bacteriol. 172 (1990) 5803-5815.
10. E. Umelo-Njaka, W.H. Bingle, F. Borchani, K.D. Le, P. Awram, T. Blake, J.F. Nomellini, J. Smit, Caulobacter crescentus synthesizes an S-layer-editing metalloprotease possessing a domain sharing sequence similarity with its paracrystalline S-layer protein, J. Bacteriol. 184 (2002) 2709-2718.
11. U. Baumann, Serralysin, in: Handbook of proteolytic enzymes, A.J. Barrett, N.D. Rawlings, J.F. Woessner (Eds.), Academic press, London, pp. 1147-1150.
12. A.W. Anderson, H.C. Nordon, R.F. Cain, G. Parrish, D. Duggan, Studies on a radio-resistant micrococcus. I. Isolation, morphology, cultural characteristics, and resistance to gamma radiation, Food Technol. 10 (1956) 575-578.
13. J.R. Battista, Against all odds: the survival strategies of Deinococcus radiodurans, Annu. Rev. Microbiol. 51 (1997) 203-224.
14. O. White, J.A. Eisen, J.F. Heidelberg, E.K. Hickey, J.D. Peterson, R.J. Dodson, D.H. Haft, M.L. Gwinn, W.C. Nelson, D.L. Richardson, K.S. Moffat, H. Qin, L. Jiang, W. Pamphile, M. Crosby, M. Shen, J.J. Vamathevan, P. Lam, L. McDonald, T. Utterback, C. Zalewski, K.S. Makarova, L. Aravind, M.J. Daly, K.W. Minton, R.D. Fleischmann, K.A. Ketchum, K.E. Nelson, S. Salzberg, H.O. Smith, J.C. Venter, C.M. Fraser, Genome sequence of the radioresistant bacterium Deinococcus radiodurans R1, Science. 286 (1999) 1571-1577.
15. K.S. Makarova, L. Aravind, Y.I. Wolf, R.L. Tatusov, K.W. Minton, E.V. Koonin, M.J. Daly, Genome of the extremely radiation-resistant bacterium Deinococcus radiodurans viewed from the perspective of comparative genomics, Microbiol. Mol. Biol. Rev. 65 (2001) 44-79.
16. K.S. Makarova, M.V. Omelchenko, E.K. Gaidamakova, V.Y. Matrosova, A. Vasilenko, M. Zhai, A. Lapidus, A. Copeland, E. Kim, M. Land, K. Mavromatis, S. Pitluck, P.M. Richardson, C. Detter, T. Brettin, E. Saunders, B. Lai, B. Ravel, K.M. Kemner, Y.I. Wolf, A. Sorokin, A.V. Gerasimova, M.S. Gelfand, J.K. Fredrickson, E.V. Koonin, M.J. Daly, Deinococcus geothermalis: the pool of extremeradiation resistance genes shrinks, PLosOne 9 (2007) e955.
17. A. Venkateswaran, S.C. McFarlan, D. Ghosal, K.W. Minton, A. Vasilenko, K. Makarova, L.P. Wackett, M.J. Daly, Physiologic determinants of radiation resistance in Deinococcus radiodurans, Appl. Environ. Microbiol. 66 (2000) 2620-2626.
18. B. Joshi, R. Schmid, K. Altendorf, S.K. Apte, Protein recycling is a major component of post-irradiation recovery in Deinococcus radiodurans strain R1, Biochem. Biophys. Res. Commun. 320 (2004) 1112-1117.
19. C. Heussen, E.B. Dowdle, Electrophoretic analysis of plasminogen activators in polyacrylamide gels containing sodium dodecyl sulfate and copolymerized substrates, Anal. Biochem. 102 (1980) 196-202.
20. G.L. Peterson, A simplification of the protein assay method of Lowry et al. which is more generally applicable, Anal. Biochem. 83 (1977) 346-356.
21. P.H. O'Farrell, High resolution two-dimensional electrophoresis of proteins, J. Biol. Chem. 250 (1975) 4007-4021.
22. K.S. Udupa, P.A. O'Cain, V. Mattimore, J.R. Battista, Novel ionizing radiation-sensitive mutants of Deinococcus radiodurans, J. Bacteriol. 176 (1994) 7439-7446.
23. A. Marchler-Bauer, J.B. Anderson, P.F. Cherukuri, C. DeWeese-Scott, L.Y. Geer, M. Gwadz, S. He, D.I. Hurwitz, J.D. Jackson, Z. Ke, C.J. Lanczycki, C.A. Liebert, C. Liu, F. Lu, G.H. Marchler, M. Mullokandov, B.A. Shoemaker, V. Simonyan, J.S. Song, P.A. Thiessen, R.A. Yamashita, J.J. Yin, D. Zhang, S.H. Bryant, CDD: a Conserved Domain Database for protein classification, Nucleic Acids Res. 33 (2005) D192-D196.
24. N.D. Rawlings, F.R. Morton, A.J. Barrett, MEROPS: the peptidase database, Nucleic Acids Res. 34 (2006) D270-D272.
25. M. Nakajima, K. Mizusawa, F. Yoshida, Purification and properties of an extracellular proteinase of psychrophilic Escherichia freundii, Eur. J. Biochem. 44 (1974) 87-96.
26. J.D. Thompson, D.G. Higgins, T.J. Gibson, CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice, Nucleic Acids Res. 22 (1994) 4673-4680.
27. D. Lyerly, A. Kreger, Purification and characterization of a Serratia marcescens metalloprotease, Infect Immun. 24 (1979) 411-421.
28. P. Vollmer, I. Walev, S. Rose-John, S. Bhakdi, Novel pathogenic mechanism of microbial metalloproteinases: liberation of membrane-anchored molecules in biologically active form exemplified by studies with the human interleukin-6 receptor, Infect Immun. 64 (1996) 3646-3651.
29. K. Morihara, J.Y. Homma, Pseudomonas proteases, in: I.A. Holder (Ed.), Bacterial enzymes and virulence, CRC Press, Boca Raton, 1985, pp. 41-79.
30. S. Létoffé, P. Delepelaire, C. Wandersman, Protease secretion by Erwinia chrysanthemi: the specific secretion functions are analogous to those of Escherichia coli alpha-haemolysin, EMBO J. 9 (1990) 1375-1382.
31. L.M. Loomes, B.W. Senior, M.A. Kerr, A proteolytic enzyme secreted by Proteus mirabilis degrades immunoglobulins of the immunoglobulin A1 (IgA1), IgA2, and IgG isotypes, Infect Immun. 58 (1990) 1979-1985.
32. U. Baumann, S. Wu, K.M. Flaherty, D.B. McKay, Three-dimensional structure of the alkaline protease of Pseudomonas aeruginosa: a two-domain protein with a calcium binding parallel beta roll motif, EMBO J. 12 (1993) 3357-3364.
33. T.M. Misenheimer, D.F. Mosher, Calcium ion binding to thrombospondin 1, J. Biol. Chem. 270 (1995) 1729-1733.
34. K.H.M. van Wely, J. Swaving, R. Freudl, A.J.M. Driessen, Translocation of proteins cross the cell envelope of Gram-positive bacteria, FEMS Microbiol Reviews 25 (2001) 437-454.
35. J.D. Bendtsen, H. Nielsen, G. von Heijne, S. Brunak, Improved prediction of signal peptides: SignalP 3.0, J. Mol. Biol. 340 (2004) 783-795.
36. K. Nakai, P. Horton, PSORT: a program for detecting sorting signals in proteins and predicting their subcellular localization, Trends. Biochem. Sci. 24 (1999) 34-36.
37. J.D. Bendtsen, L. Kiemer, A. Fausbøll, S. Brunak, Non-classical protein secretion in bacteria, BMC Microbiol. 5 (2005) 58.