In vitro refolding of carboxypeptidase T precursor from Thermoactinomyces vulgaris obtained in Escherichia coli as cytoplasmic inclusion bodies

Protein Expression and Purification

Volumn 40, Issue 1, 2005, Pages 51-59

  Trachuk, Lesya ^a   Letarov, Andrei ^a   Kudelina, Irina A ^b   Yusupova, Margarita P ^a   Chestukhina, Galina G ^a  

^a STATE RESEARCH INSTITUTE OF GENETICS AND SELECTION OF INDUSTRIAL MICROORGANISMS   (Russian Federation)

^b SHEMYAKIN OVCHINNIKOV INSTITUTE OF BIOORGANIC CHEMISTRY   (Russian Federation)

Author keywords

Carboxypeptidase; Refolding; Zymogen

Indexed keywords

ESCHERICHIA COLI; THERMOACTINOMYCES VULGARIS;

EID: 13844296646     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2004.10.020     Document Type: Article

References (25)

1. F.X. Aviles, J. Vendrell, A. Guasch, M. Coll, and R. Huber Advances in metallo-procarboxypeptidases. Emerging details on the inhibition mechanism and on the activation process Eur. J. Biochem. 211 1993 381 389
2. A.L. Osterman, V.M. Stepanov, G.N. Rudenskaya, O.M. Khodova, and I.A. Tsaplina Carboxypeptidase T: extracellular carboxypeptidase of thermoactinomycetes-a distant analog of animal carboxypeptidases Biochemistry (USSR) 49 1984 292 301
3. S.V. Smulevitch, A.L. Osterman, O.V. Galperina, M.V. Matz, and V.M. Stepanov Molecular cloning and primary structure of Thermoactinomyces vulgaris carboxypeptidase T, a metalloenzyme endowed with dual substarte specificity FEBS Lett. 291 1991 75 78
4. A.L. Osterman, N.V. Grishin, S.V. Smulevich, M.V. Matz, and V.M. Stepanov Primary structure of carboxypeptidase T: delineation of functionally relevant features in Zn-carboxypeptidase family J. Prot. Chem. 11 1992 561 570
5. Y. Narahashi The amino acid sequence of zinc-carboxypeptidase from Streptomyces griseus J. Biochem. 107 1990 879 886
6. A.M. Bushueva, A.B. Shevelev, J. Gumpert, G.G. Chestukhina, and V.M. Stepanov Expression of he carboxypeptidase T gene from Thermoactinomyces vulgaris in stable protoplast type L-forms of Proteus mirabilis FEMS Microbiol. Lett. 159 1998 145 150
7. J. Eder, and A.R. Fersht Pro-sequence-assisted protein folding Mol. Microbiol. 16 1995 609 614
8. M.A. Phillips, and W.J. Rutter Role of the prodomain in folding and secretion of rat pancreatic carboxypeptidase A1 Biochemistry 35 1996 6771 6776
9. L. Song, and L.D. Fricker Calcium- and pH-dependent aggregation of carboxypeptidase E J. Biol. Chem. 270 1995 7963 7967
10. I.P. Morozova, M.P. Yusupova, M.Y. Gololobov, N.V. Korolkova, and V.M. Stepanov Metalloproteinase of Bacillus mesentericus str. V-313 Biochemistry (USSR) 85 1993 1420 1429
11. M.P. Yusupova, S.A. Novgorodova, and V.M. Stepanov Sequential attachment of arginine residues to peptides catalyzed by subtilisin Bioorg. Khim. (USSR) 22 1996 589 595
12. U.K. Laemmli Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227 1970 680 685
13. S.W. Provencher A constrained regularisation method for inverting data represented by linear algebraic or integral equations Comput. Phys. Commun. 27 1982 213 227
14. A. Mitraki, and J. King Protein folding intermediates and inclusion body formation Biotechnology 7 1989 690 697
15. A. Teplyakov, K. Polyakov, G. Obmolova, A. Osterman, and V. Stepanov Crystal strtucture of carboxypeptidase T from Thermoactinomyces vulgaris Eur. J. Biochem. 208 1992 281 288
16. C.H. Schein Solubility as a function of protein structure and solvent components Biotechnology 8 1990 308 315
17. T.I. Vaganova, N.P. Medvedeva, and V.M. Stepanov Renaturation of bacterial metalloproteinases Biochemistry (USSR) 58 1993 913 920
18. T.E. Creighton, N.J. Darby, and J. Kemmink The roles of partly folded intermediates in protein folding FASEB J. 10 1996 110 118
19. C. Marie-Claire, B.P. Roques, and A. Beaumont Intramolecular processing of pro-thermolysin J. Biol. Chem. 273 1998 5697 5701
20. 2+ in subtilisin maturation J. Biochem. 131 2002 31 37
21. J.L. Sohl, S.S. Jaswal, and D.A. Agard Unfolded conformations of alpha-lytic protease are more stable than its native state Nature 395 1998 817 819
22. B. Ruan, J. Hoskins, and P.N. Bryan Rapid folding of calcium-free subtilisin by a stabilized pro-domain mutant Biochemistry 38 1999 8562 8571
23. I. Garcia-Saez, D. Reverter, J. Vendrell, F.X. Aviles, and M. Coll The three-dimensional structure of human pro-carboxypeptidase A2. Deciphering the basis of the inhibition, activation and intrinsic activity of the zymogen EMBO J. 16 1997 6906 6913
24. L.A. Trachuk, A.M. Bushueva, A.B. Shevelev, S.A. Novgorodova, V.Kh. Akparov, and G.G. Chestukhina Characterization of S1′ subsite specificity of Thermoactinomyces vulgaris carboxypeptidase T by site-directed mutagenesis Vopr. Med. Khim. (Russia) 48 2002 577 585
25. V.M. Stepanov Carboxypeptidase T Methods Enzymol. 248 1995 675 683