A novel secreted metzincin metalloproteinase from Bacillus intermedius

FEBS Letters

Volumn 584, Issue 21, 2010, Pages 4419-4425

  Sabirova, Albina R ^a   Rudakova, Natalya L ^a   Balaban, Nelly P ^a   Ilyinskaya, Olga N ^a   Demidyuk, Ilya V ^b   Kostrov, Sergey V ^b   Rudenskaya, Galina N ^c   Sharipova, Margarita R ^a  

^a KAZAN FEDERAL UNIVERSITY   (Russian Federation)

^b INSTITUTE OF MOLECULAR GENETICS   (Russian Federation)

^c MOSCOW STATE UNIVERSITY   (Russian Federation)

Author keywords

ADAM like proteinase; Bacillus intermedius; Gene expression; HEXXHXXGXXH motif; Metalloproteinase; Molecular cloning; Protein purification

Indexed keywords

METALLOPROTEINASE; METHIONINE; METZINCIN; PROTEINASE; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; BACILLUS; BACILLUS INTERMEDIUS; BACILLUS SUBTILIS; BACTERIAL GENE; CONTROLLED STUDY; ENZYME ACTIVE SITE; EUKARYOTE; GENE EXPRESSION; MPRBI GENE; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROKARYOTE; PROTEIN DOMAIN; PROTEIN MOTIF; PROTEIN PURIFICATION; PROTEIN STRUCTURE;

AMINO ACID SEQUENCE; ANIMALS; BACILLUS; BASE SEQUENCE; CLONING, MOLECULAR; EXTRACELLULAR SPACE; HUMANS; METALLOENDOPEPTIDASES; METALLOPROTEASES; MOLECULAR SEQUENCE DATA; PROTEIN STRUCTURE, TERTIARY; SEQUENCE ALIGNMENT; SEQUENCE ANALYSIS, DNA;

BACILLUS INTERMEDIUS; BACILLUS SUBTILIS; EUKARYOTA; PROKARYOTA;

EID: 78049314692     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2010.09.049     Document Type: Article

References (33)

1. Barrett A.J., Rawlings N.D. Perspectives in biochemistry and biophysics. Families and clans of serine peptidases. Arch. Biochem. Biophys. 1995, 318(2):247-250.
2. Oberholzer A.E., Bumann M., Hede T., Russo S., Baumann U. Metzincin's canonical methionine is responsible for the structural integrity of the zinc-binding site. Biol. Chem. 2009, 390:875-881.
3. Gomis-Rüth F.X. Catalytic domain architecture of metzincin metalloproteinases. J. Biol. Chem. 2009, 284(23):15353-15357.
4. Gomis-Rüth F.X. Structural aspects of the metzincin clan of metalloendopeptidases. Mol. Biotechnol. 2003, 24:157-202.
5. Stöcker W., Grams F., Baumann U., Reinemer P., Gomis-Rüth F.X., McKay D.B., Bode W. The metzincins - topological and sequential relations between the astacins, adamalysins, serralysins, and matrixins (collagenases) define a superfamily of zinc-peptidases. Protein Sci. 1995, 4:823-840. PMID:7663339.
6. Sterchi E.E., Stöcker W., Bond J.S. Meprins, membrane-bound and secreted astacin metalloproteinases. Mol. Aspects Med. 2008, 29:309-328.
7. Jiang W., Bond J.S. Families of metalloendopeptidases and their relationships. FEBS Lett. 1992, 312(2,3):110-114.
8. Bode W., Gomis-Rüth F.-X., Huber R., Zwilling R., Stöcker W. Structure of astacin and implications for activation of astacins and zinc-ligation of collagenases. Nature 1992, 358:164-167.
9. Yiallouros I., Kappelhoff R., Schilling O., Wegmann F., Helms M.W., Auge A., Brachtendorf G., Berkhoff E.G., Beermann B., Hinz H.J., König S., Peter-Katalinic J., Stöcker W. Activation mechanism of pro-astacin: role of the pro-peptide, tryptic and autoproteolytic cleavage and importance of precise amino-terminal processing. J. Mol. Biol. 2002, 342(2):237-246.
10. Guevara T., Yiallouros I., Kappelhoff R., Bissdorf S., Stöcker W., Gomis-Rüth F.-X. Proenzyme structure and activation of astacin metallopeptidase. J. Biol. Chem. 2010, 285(18):13958-13965.
11. Grams F., Huber R., Kress L.F., Moroder L., Bode W. Activation of snake venom metalloproteinases by a cysteine switch-like mechanism. FEBS Lett. 1993, 335(1):76-80.
12. Seals D.F., Courtneidge S.A. The ADAMs family of metalloproteases: multidomain proteins with multiple functions. Genes Dev. 2003, 17(1):7-30.
13. Balaban N., Gabdrakhmanova L., Sharipova M., Sokolova E., Malikova L., Mardanova A., Rudenskaya G., Leshchinskaya I. Selection of cultivation medium for production of late stationary phase serine proteinases from Bacillus intermedius. J. Basic Microbiol. 2004, 44(6):415-423.
14. Sharipova M.R., Shagimardanova E.I., Chastukhina I.B., Shamsutdinov T.R., Balaban N.P., Mardanova A.M., Rudenskaya G.N., Demidyuk I.V., Kostrov S.V. The expression of Bacillus intermedius glutamyl endopeptidase gene in Bacillus subtilis recombinant strains. Mol. Biol. Rep. 2007, 34:79-87.
15. Sharipova M., Balaban N., Kayumov A., Kirillova Yu., Mardanova A., Gabdrakhmanova L., Leshchinskaya I., Rudenskaya G., Akimkina T., Safina D., Demidyuk I., Kostrov S. The expression of the serine proteinase of Bacillus intermedius in Bacillus subtilis. Microbiol. Res. 2008, 163:39-50.
16. Leshchinskaya I.B., Shakirov E.V., Itskovitch E.L., Balaban N.P., Mardanova A.M., Sharipova M.R., Viryasov M.B., Rudenskaya G.N., Stepanov V.M. Glutamyl endopeptidase of Bacillus intermedius, strain 3-19. FEBS Lett. 1997, 404:241-244.
17. Balaban N.P., Mardanova A.M., Sharipova M.R., Gabdrakhmanova L.A., Garusov A.V., Milgotina E.I., Rudenskaya G.N., Leshchinskaya I.B. Isolation and characterization of glutamyl endopeptidase 2 from Bacillus intermedius 3-19. Biochemistry (Moscow) 2003, 68(11):1217-12224.
18. Mikhailova E.O., Balaban N.P., Mardanova A.M., Rudakova N.L., Ilyinskaya O.N., Rudenskaya G.N., Rizvanov A.A., Sharipova M.R. Purification of subtilisin-like serine proteinase from recombinant Bacillus subtilis during different phases of growth. Ann. Microbiol. 2009, 59(2):1-8.
19. Balaban N.P., Mardanova A.M., Sharipova M.R., Gabdrakhmanova L.A., Sokolova E.A., Rudenskaya G.N., Leshchinskaya I.B. Purification and characterization of serine proteinase 2 from Bacillus intermedius 3-19. Biochemistry (Moscow) 2004, 69(4):420-426.
20. Sorokin A.V., Khazak V.E. Expression unit in the region of replication initiation in the streptococcal plasmid pSM19035. Mol. Biol. (Mosc). 1990, 24(4):993-1000.
21. Rebrikov D.V., Akimkina T.V., Shevelev A.B., Demidyuk I.V., Bushueva A.M., Kostrov S.V., Rudenskaya G.N., Stepanov V.M. Bacillus intermedius glutamyl endopeptidase. Molecular cloning and nucleotide sequence of the structural gene. J. Protein Chem. 1999, 18(1):21-27.
22. Yang M.Y., Ferrari E., Henner D.J. Cloning of the neutral protease gene of Bacillus subtilis and the use of the cloned gene to crate an in vitro-derived deletion mutation. J. Bacteriol. 1984, 160(1):15-21.
23. Altschul S.F., Madden T.L., Schäffer A.A., Zhang J., Zhang Z., Miller W., Lipman D.J. Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res. 1997, 25(17):3389-3402.
24. Bode W., Grams F., Reinemer P., Gomis-Rüth F.-X., Baumann U., McKay D.B., Stöcker W. The metzincin-superfamily of zinc-peptidases. Adv. Exp. Med. Biol. 1996, 389:1-11.
25. Grams F., Dive V., Yiotakis A., Yiallouros I., Vassiliou S., Zwilling R., Bode W., Stöcker W. Structure of astacin with a transition-state analog inhibitor. Nature Struct. Biol. 1996, 3:671-675.
26. Hede T., Baumann U. Proteinase C of Erwinia chrisantemi: the crystal structure and role of amino acids Y228 and E189. J. Mol. Biol. 2001, 314:187-193.
27. Stöker W., Bode W. Structural features of a superfamily of zinc-endopeptidases: the metzincins. Curr. Opin. Struct. Biol. 1995, 5(3):383-390.
28. Cruz-Munor W., Khokha R. The role of tissue inhibitors of metalloendopeptidases in tumorogenesis and metastasis. Critical Rev. Clinical Lab. Sci. 2008, 43(3):291-338.
29. Tallant C., Marrero A., Gomis-Rüth F.-X. Matrix metalloproteinases: fold and function of their catalytic domains. BBA 2010, 1803(1):20-28.
30. Li X., Liu Q., Zhou T., Zhao S., Zhou S. PAPP-A: a possible pathogenic link to the instability of atherosclerotic plaque. Med. Hypotheses 2008, 70:597-599.
31. Matsui T., Fulimura Y., Titani K. Snake venom proteinases affecting hemostasis and thrombosis. Biochim. Biophys. Acta 2000, 1477:146-156.
32. Ge G., Greenspan D.S. Development roles of the BMP1/TLD metalloproteinases. Birth Defects Res. C 2006, 78:47-68.
33. Lopez-Otin C., Bond J.S. Proteases: multifunctional enzymes in life and disease. J. Biol. Chem. 2008, 283(45):30433-30437.