Molecular cloning and sequence analysis of a novel zinc-metalloprotease gene from the Salinivibrio sp. strain AF-2004 and its extracellular expression in E. coli

Gene

Volumn 408, Issue 1-2, 2008, Pages 196-203

  Karbalaei Heidari, Hamid Reza ^a,c   Ziaee, Abed Ali ^a   Amoozegar, Mohammad Ali ^b   Cheburkin, Yuri ^c   Budisa, Nediljko ^c  

^a UNIVERSITY OF TEHRAN   (Iran)

^b University College of Science   (Iran)

^c MAX PLANCK INSTITUTE OF BIOCHEMISTRY   (Germany)

Author keywords

Moderately halophilic bacteria; Nucleotide sequence; Protease; Salinivibrio; Zinc binding motif

Indexed keywords

ALANINE; AMINO ACID; CASEIN; ELASTASE; ISOPROPYL 1 THIO BETA DEXTRO GALACTOPYRANOSIDE; METALLOPROTEINASE; PYRANOSIDE; TRYPSIN; UNCLASSIFIED DRUG; ZINC METALLOPROTEINASE;

AMINO ACID SEQUENCE; ARTICLE; BACTERIAL STRAIN; BASE PAIRING; CARBOXY TERMINAL SEQUENCE; CONSENSUS SEQUENCE; ELECTROSPRAY MASS SPECTROMETRY; ENZYME INDUCTION; ESCHERICHIA COLI; GENE EXPRESSION PROFILING; GENE EXPRESSION REGULATION; GENE INSERTION SEQUENCE; GENE OVEREXPRESSION; GENE SEQUENCE; HALOPHILIC BACTERIUM; MOLECULAR CLONING; MOLECULAR WEIGHT; NONHUMAN; NUCLEOTIDE SEQUENCE; OPEN READING FRAME; PLASMID; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN MOTIF; PROTEIN PURIFICATION; SALINIVIBRIO; SEQUENCE ALIGNMENT; SEQUENCE ANALYSIS; SEQUENCE HOMOLOGY;

AMINO ACID SEQUENCE; BASE SEQUENCE; CLONING, MOLECULAR; ESCHERICHIA COLI; GENES, BACTERIAL; METALLOPROTEASES; MOLECULAR SEQUENCE DATA; SEQUENCE ANALYSIS; VIBRIONACEAE; ZINC;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; PSEUDOMONAS AERUGINOSA; SALINIVIBRIO; VIBRIO VULNIFICUS;

EID: 37549005219     PISSN: 03781119     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.gene.2007.11.002     Document Type: Article

References (35)

1. Amoozegar M.A., Fatemi A.Z., Karbalaei-Heidari H.R., and Razavi M.R. Production of an extracellular alkaline metalloprotease from a newly isolated, moderately halophile, Salinivibrio sp. strain AF-2004. Microbiol. Res. 162 (2007) 369-377
2. Cheng J.C., Shao C.P., and Hor L.I. Cloning and nucleotide sequencing of the protease gene of Vibrio vulnificus. Gene 183 (1996) 255-257
3. Coronado M.J., Vargas C., Mellado E., Tegos G., Drainas C., Nieto J.J., and Ventosa A. The alpha-amylase gene amyH of the moderate halophile Halomonas meridiana: cloning and molecular characterization. Microbiology 146 (2000) 861-868
4. Cotik V., Remero Zaliz R., and Zwir I. A hybrid promoter analysis methodology for prokaryotic genomes. Fuzzy Sets Syst. 152 (2005) 83-102
5. David V.A., Deutch A.H., Sloma A., Pawlyk D., Ally A., and Durham D.R. Cloning, sequencing and expression of the gene encoding the extracellular neutral protease, vibriolysin, of Vibrio proteolyticus. Gene 112 (1992) 107-112
6. Dalbry R.E. Leader peptidase. Mol. Microbiol. 5 (1991) 2855-2860
7. Filloux A. The underlying mechanisms of type II protein secretion. Biochem. Biophys. Acta 1694 (2004) 163-179
8. Ghandbhir M., Rasched I., Marlie're P., and Mutzel R. Convergent evolution of amino acid usage in archaebacterial and eubacterial lineages adapted to high salt. Res. Microbiol. 146 (1995) 113-120
9. Gray L., Mackman N., Nicaud J.M., and Holland I.B. The carboxy-terminal region of haemolysin 2001 is required for secretion of the toxin from Escherichia coli. Mol. Gen. Genet. 205 (1986) 127-133
10. Häse C.C., and Finkelstein R.A. Cloning and nucleotide sequence of the Vibrio cholerae hemagglutinin/protease (HA/protease) gene and construction of an HA/protease negative strain. J. Bacteriol. 173 (1991) 3311-3317
11. Häse C.C., and Finkelstein R.A. Bacterial extracellular zinc-containing metalloproteases. Microbiol. Rev. 57 (1993) 823-837
12. Horikoshi K. Alkaliphiles: some applications of their products for biotechnology. Microbiol. Mol. Biol. Rev. 63 (1999) 735-750
13. Jacobs M., Eliasson M., Uhlen M., and Flock J.-I. Cloning, sequencing and expression of subtilisin Carlsberg from Bacillus licheniformis. Nucleic Acids Res. 13 (1985) 8913-8926
14. Kim S.-K., Yang J.-Y., and Cha J. Cloning and sequence analysis of a novel metalloprotease gene from Vibrio parahaemolyticus 04. Gene 283 (2002) 277-286
15. Karlin S., and Zhu Z.-Y. Classification of mononuclear zinc metal sites in protein structures. Proc. Natl. Acad. Sci. U. S. A. 94 (1997) 14231-14236
16. Karbalaei-Heidari H.R., Ziaee A.-A., Schaller J., and Amoozegar M.A. Purification and characterization of an extracellular haloalkaline protease produced by the moderately halophilic bacterium, Salinivibrio sp. strain AF-2004. Enzyme Micobiol. Technol. 40 (2007) 266-272
17. Karbalaei-Heidari H.R., Ziaee A.-A., and Amoozegar M.A. Purification and biochemical characterization of a protease secreted by the Salinivibrio sp. strain AF-2004 and its behavior in organic solvents. Extremophiles 11 (2007) 237-243
18. Kushner D.J. Life in high salt and solute concentrations: halophilic bacteria. In: Kushner D.J. (Ed). Microbial Life In Extreme Environments (1978), Academic Press, Ltd., London, United Kingdom 317-368
19. Lee C., Su S., and Liaw R. Molecular analysis of an extracellular protease gene from Vibrio parahaemolyticus. Microbiology 141 (1995) 2569-2576
20. McPhalen C.A., Strynadka N.C., and James M.N. Calcium-binding sites in proteins: a structural perspective. Adv. Protein Chem. 42 (1991) 77-144
21. Mijts B.N., and Patel B.K. Cloning, sequencing and expression of an alpha-amylase gene, amyA, from the thermophilic halophile Halothermothrix orenii and purification and biochemical characterization of the recombinant enzyme. Microbiology 148 (2002) 2343-2349
22. Milton D.L., Norqvist A., and Wolf-Watz H. Cloning of a metalloprotease gene involved in the virolence mechanism of Vibrio anguillarum. J. Bacteriol. 174 (1992) 7235-7244
23. Miyoshi S., and Shinoda S. Microbial metalloproteases and pathogenesis. Microbes Infect. 2 (2000) 91-98
24. Miyoshi S., Kawata K., Tomochika K., Shinoda S., and Yamamoto S. The C-terminal domain promotes the hemorrhagic damage caused by Vibrio vulnificus metalloprotease. Toxicon 39 (2001) 1883-1886
25. Niehaus F., Bertoldo C., Kähler M., and Antranikian G. Extremophiles as a source of novel enzymes for industrial application. Appl. Microbiol. Biotechnol. 51 (1999) 711-729
26. Oneda H., and Inouye K. Refolding and recovery of recombinant human matrilysin metalloproteinase 7 (matrilysin) from inclusion bodies expressed by Escherichia coli. J. Biochem. 126 (1999) 905-911
27. Pugsley A.P. The complete general secretory pathway in gram-negative bacteria. Microbiol. Rev. 57 (1993) 50-108
28. Sloma A., Rudolph C.F., Rufo G.A., Sullivan B.J., Theriault K.A., Ally D., and Pero J. Gene encoding a novel extracellular metalloprotease in Bacillus subtilis. J. Bacteriol. 172 (1990) 1024-1029
29. Thompson J.D., Higgins D.G., and Gibson T.J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighing, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22 (1994) 4673-4680
30. Takahashi T., Kenneth K.-S.Ng., Oyama H., and Kohei O. Molecular cloning of the gene encoding Vibrio metalloprotease vimelysin and isolation of a mutant with high stability in organic solvents. J. Biochem. 138 (2005) 701-710
31. Teo J.W.P., Zhang L.H., and Poh C.L. Cloning and characterization of a metalloprotease from Vibrio harveyi strain AP6. Gene 303 (2003) 147-156
32. Thayer M.M., Flaherty K.M., and McKay D.B. Three-dimensional structure of the elastase of Pseudomonas aeruginosa at 1.5-A° resolution. J. Biol. Chem. 266 (1991) 2864-2871
33. Trachuk L., Letarov A., Kudelina I.A., Yusupova M.P., and Chestukhina G.G. In vitro refolding of carboxypeptidase T precursor from Thermoactinomyces vulgaris obtained in Escherichia coli as cytoplasmic inclusion bodies. Protein Expr. Purif. 40 (2005) 51-59
34. Ventosa A., Nieto J.J., and Oren A. Biology of moderately halophilic aerobic bacteria. Microbiol. Mol. Biol. Rev. 62 (1998) 504-544
35. Veltman O.R., Vriend G., Berendsen H.J., van den Burg B., Venema G., and Eijsink V.G. A single calcium binding site is crucial for the calcium-dependent thermal stability of thermolysin-like proteases. Biochemistry 37 (1998) 5312-5319