Processing of protealysin precursor

Biochimie

Volumn 91, Issue 5, 2009, Pages 639-645

  Gromova, Tania Yu ^a   Demidyuk, Ilya V ^a   Kozlovskiy, Viacheslav I ^b   Kuranova, Inna P ^c   Kostrov, Sergey V ^a  

^a INSTITUTE OF MOLECULAR GENETICS   (Russian Federation)

^b SEMENOV INSTITUTE OF CHEMICAL PHYSICS   (Russian Federation)

^c SHUBNIKOV INSTITUTE OF CRYSTALLOGRAPHY   (Russian Federation)

Author keywords

Processing; Protealysin precursor; Serratia proteamaculans; Thermolysin like protease

Indexed keywords

ALANINE; GLUTAMINE; MUTANT PROTEIN; POLYHISTIDINE TAG; PROTEALYSIN; PROTEIN PRECURSOR; PROTEINASE; SUBTILISIN; THERMOLYSIN; UNCLASSIFIED DRUG;

AMINO ACID SUBSTITUTION; AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CATALYSIS; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME DEGRADATION; GENE EXPRESSION; MOLECULAR DYNAMICS; NONHUMAN; PROTEIN PROCESSING; PROTEIN PURIFICATION;

BACTERIAL PROTEINS; GENETIC VECTORS; HYDROGEN-ION CONCENTRATION; KINETICS; PROTEIN PRECURSORS; SERRATIA; THERMOLYSIN;

SERRATIA PROTEAMACULANS;

EID: 64049100537     PISSN: 03009084     EISSN: 61831638     Source Type: Journal    
DOI: 10.1016/j.biochi.2009.03.008     Document Type: Article

References (30)

1. Demidyuk I.V., Kalashnikov A.E., Gromova T.Y., Gasanov E.V., Safina D.R., Zabolotskaya M.V., Rudenskaya G.N., and Kostrov S.V. Cloning, sequencing, expression, and characterization of protealysin, a novel neutral proteinase from Serratia proteamaculans representing a new group of thermolysin-like proteases with short N-terminal region of precursor. Protein. Expr. Purif. 47 (2006) 551-561
2. Rawlings N.D., and Barrett A.J. Evolutionary families of metallopeptidases. Methods. Enzymol. 248 (1995) 183-228
3. Demidyuk I.V., Gasanov E.V., Safina D.R., and Kostrov S.V. Structural organization of precursors of thermolysin-like proteinases. Protein J. 27 (2008) 343-354
4. Kyostio S.R., Cramer C.L., and Lacy G.H. Erwinia carotovora subsp. carotovora extracellular protease: characterization and nucleotide sequence of the gene. J. Bacteriol. 173 (1991) 6537-6546
5. Wang H., and Dowds B.C. Phase variation in Xenorhabdus luminescens: cloning and sequencing of the lipase gene and analysis of its expression in primary and secondary phases of the bacterium. J. Bacteriol. 175 (1993) 1665-1673
6. Held K.G., LaRock C.N., D'Argenio D.A., Berg C.A., and Collins C.M. A metalloprotease secreted by the insect pathogen Photorhabdus luminescens induces melanization. Appl. Environ. Microbiol. 73 (2007) 7622-7628
7. Kwon Y.T., Lee H.H., and Rho H.M. Cloning, sequencing, and expression of a minor protease-encoding gene from Serratia marcescens ATCC21074. Gene 125 (1993) 75-80
8. Grimont F., and Grimont P. The Genus Serratia. In: Dworkin M. (Ed). The Prokaryotes vol. 6 (2006), Springer, New York 219-244
9. Jackson T.A., Boucias D.G., and Thaler J.O. Pathobiology of amber disease, caused by Serratia spp., in the New Zealand grass grub, Costelytra zealandica. J. Invertebr. Pathol. 78 (2001) 232-243
10. Bollet C., Grimont P., Gainnier M., Geissler A., Sainty J.M., and De Micco P. Fatal pneumonia due to Serratia proteamaculans subsp. quinovora. J. Clin. Microbiol. 31 (1993) 444-445
11. Efremova T., Ender N., Brudnaja M., Komissarchik Y., and Khaitlina S. Specific invasion of transformed cells by Escherichia coli A2 strain. Cell. Biol. Int. 25 (2001) 557-561
12. Bozhokina E., Khaitlina S., and Adam T. Grimelysin, a novel metalloprotease from Serratia grimesii, is similar to ECP32. Biochem. Biophys. Res. Commun. 367 (2008) 888-892
13. McIver K.S., Kessler E., Olson J.C., and Ohman D.E. The elastase propeptide functions as an intramolecular chaperone required for elastase activity and secretion in Pseudomonas aeruginosa. Mol. Microbiol. 18 (1995) 877-889
14. Braun P., Tommassen J., and Filloux A. Role of the propeptide in folding and secretion of elastase of Pseudomonas aeruginosa. Mol. Microbiol. 19 (1996) 297-306
15. Marie-Claire C., Ruffet E., Beaumont A., and Roques B.P. The prosequence of thermolysin acts as an intramolecular chaperone when expressed in trans with the mature sequence in Escherichia coli. J. Mol. Biol. 285 (1999) 1911-1915
16. Tang B., Nirasawa S., Kitaoka M., Marie-Claire C., and Hayashi K. General function of N-terminal propeptide on assisting protein folding and inhibiting catalytic activity based on observations with a chimeric thermolysin-like protease. Biochem. Biophys. Res. Commun. 301 (2003) 1093-1098
17. Serkina A.V., Gorozhankina T.F., Shevelev A.B., and Chestukhina G.G. Propeptide of the metalloprotease of Brevibacillus brevis 7882 is a strong inhibitor of the mature enzyme. FEBS Lett. 456 (1999) 215-219
18. O'Donohue M.J., and Beaumont A. The roles of the prosequence of thermolysin in enzyme inhibition and folding in vitro. J. Biol. Chem. 271 (1996) 26477-26481
19. Kessler E., and Safrin M. The propeptide of Pseudomonas aeruginosa elastase acts an elastase inhibitor. J. Biol. Chem. 269 (1994) 22726-22731
20. Wetmore D.R., Wong S.L., and Roche R.S. The role of the pro-sequence in the processing and secretion of the thermolysin-like neutral protease from Bacillus cereus. Mol. Microbiol. 6 (1992) 1593-1604
21. Marie-Claire C., Roques B.P., and Beaumont A. Intramolecular processing of prothermolysin. J. Biol. Chem. 273 (1998) 5697-5701
22. Bitar A.P., Cao M., and Marquis H. The metalloprotease of Listeria monocytogenes is activated by intramolecular autocatalysis. J. Bacteriol. 190 (2008) 107-111
23. McIver K., Kessler E., and Ohman D.E. Substitution of active-site His-223 in Pseudomonas aeruginosa elastase and expression of the mutated lasB alleles in Escherichia coli show evidence for autoproteolytic processing of proelastase. J. Bacteriol. 173 (1991) 7781-7789
24. Kawamoto S., Shibano Y., Fukushima J., Ishii N., Morihara K., and Okuda K. Site-directed mutagenesis of Glu-141 and His-223 in Pseudomonas aeruginosa elastase: catalytic activity, processing, and protective activity of the elastase against Pseudomonas infection. Infect. Immun. 61 (1993) 1400-1405
25. Toma S., Campagnoli S., De Gregoriis E., Gianna R., Margarit I., Zamai M., and Grandi G. Effect of Glu-143 and His-231 substitutions on the catalytic activity and secretion of Bacillus subtilis neutral protease. Protein. Eng. 2 (1989) 359-364
26. Balaban N.P., Mardanova A.M., Sharipova M.R., Gabdrakhmanova L.A., Sokolova E.A., Rudenskaya G.N., and Leshchinskaya I.B. Purification and characterization of serine proteinase 2 from Bacillus intermedius 3-19. Biochemistry (Mosc) 69 (2004) 420-426
27. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
28. Dodonov A.F., Loboda A.V., Kozlovski V.I., Soulimenkov I.V., Raznikov V.V., Zhen Z., Horwath T., and Wollnik H. High-resolution electrospray ionization orthogonal-injection time-of-flight mass spectrometer. Eur. J. Mass. Spectrom. 6 (2000) 481-490
29. Sarkar G., and Sommer S.S. The "megaprimer" method of site-directed mutagenesis. Biotechniques 8 (1990) 404-407
30. Beaumont A., O'Donohue M.J., Paredes N., Rousselet N., Assicot M., Bohuon C., Fournie-Zaluski M.C., and Roques B.P. The role of histidine 231 in thermolysin-like enzymes. A site-directed mutagenesis study. J. Biol. Chem. 270 (1995) 16803-16808