Analysis of the effect of potato carboxypeptidase inhibitor pro-sequence on the folding of the mature protein

European Journal of Biochemistry

Volumn 270, Issue 17, 2003, Pages 3641-3650

  Bronsoms, Sílvia ^a   Villanueva, Josep ^a   Canals, Francesc ^a   Querol, Enrique ^a   Aviles, Francesc X ^a  

^a UNIVERSITAT AUTÒNOMA DE BARCELONA   (Spain)

Author keywords

Disulfide; Pro region; Protease inhibitor; Protein folding; Structure

Indexed keywords

CARBOXYPEPTIDASE; CARBOXYPEPTIDASE INHIBITOR; ENZYME INHIBITOR; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CIRCULAR DICHROISM; DISULFIDE BOND; ENZYME SPECIFICITY; ESCHERICHIA COLI; IN VIVO STUDY; INHIBITION KINETICS; MASS SPECTROMETRY; MOLECULAR DYNAMICS; NONHUMAN; POTATO; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN PURIFICATION; SEQUENCE ANALYSIS;

AMINO ACID SEQUENCE; CARBOXYPEPTIDASES; CIRCULAR DICHROISM; CYSTEINE; DEUTERIUM; ENZYME PRECURSORS; ESCHERICHIA COLI; KINETICS; LEUCYL AMINOPEPTIDASE; MOLECULAR SEQUENCE DATA; MUTAGENESIS; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; OXIDATION-REDUCTION; PEPTIDE FRAGMENTS; PLANT PROTEINS; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN RENATURATION; RECOMBINANT PROTEINS; SPECTROMETRY, MASS, MATRIX-ASSISTED LASER DESORPTION-IONIZATION;

ESCHERICHIA COLI; SOLANUM TUBEROSUM;

EID: 0042324395     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1033.2003.03754.x     Document Type: Article

References (32)

1. Thomas, J.G., Ayling, A. & Baneyx, F. (1997) Molecular chaperones, folding catalysts, and the recovery of active recombinant proteins from E. coli: to fold or to refold. Appl. Biochem. Biotechnol. 66, 197-238.
2. Ferrari, D.M. & Soling, H.D. (1999) The protein disulphide-isomerase family: unravelling a string of folds. Biochem. J. 339, 1-10.
3. Gothel, S.F. & Marahiel, M.A. (1999) Peptidyl-prolyl cis-trans isomerases, a superfamily of ubiquitous folding catalysts. Cell Mol. Life Sci. 55, 423-436.
4. Martoglio, B. & Dobberstein, B. (1998) Signal sequences: more than just greasy peptides. Trends Cell Biol. 8, 410-415.
5. Shinde, U. & Inouye, M. (2000) Intramolecular chaperone: polypeptide extensions that modulate protein folding. Cell Dev. Biol. 11, 35-44.
6. Van den Hazel, H.B., Kielland-Brandt, M.C. & Winther, J.R. (1993) The propeptide is required for in vivo formation of stable active yeast proteinase A and can function even when not covalently linked to the mature region. J. Biol. Chem. 268, 18002-18007.
7. Ikemura, H., Takagi, H. & Inouye, M. (1987) Requirement of prosequence for the production of active subtyilisin E in Escherichia coli. J. Biol. Chem. 262, 7859-7864.
8. Rattenholl, A., Ruoppolo, M., Flagiello, A., Monti, M., Vinci, F., Marino, G., Lilie, H., Schwarz, E. & Rudolph, R. (2001) Prosequence assisted folding and disulfide bond formation of human neerve growth factor. J. Mol. Biol. 305, 523-533.
9. Baardsnes, J., Sidhu, S., MacLeod, A., Elliott, J., Morden, D., Watson, J. & Borgford, T. (1998) Streptomyces griseus protease B: secretion correlates with the length of the propeptide. Bacteriology 180, 3241-3244.
10. Weissman, J.S. & Kim, P.S. (1992) The pro region of BPTI facilitates folding. Cell 71, 841-851.
11. Creighton, T.E., Bagley, C.J., Cooper, L., Darby, N.J., Freedman, R.B., Kemmink, J. & Sheikh, A. (1993) On the biosynthesis of bovine pancreatic trypsin inhibitor (BPTI): structure, processing, folding and disulphide bond formation of the precursor in vitro and in microsomes. J. Mol. Biol. 232, 1176-1196.
12. Hidaka, Y., Shimono, C., Ohno, M., Okumura, N., Adermann, K., Forssmann, W.-G. & Shimonishi, Y. (2000) Dual function of the propeptide of prouroguanylin in the folding of the mature peptide. J. Biol. Chem. 275, 25155-25162.
13. Price-Carter, M., Gray, W.R. & Goldenberg, D.P. (1996) Folding of ω-conotoxins. 1. Efficient disulfide-coupled folding of mature sequence in vitro. Biochemistry 35, 15537-15546.
14. Price-Carter, M., Gray, W.R. & Goldenberg, D.P. (1996) Folding of ω-conotoxins. 1. Influence of precursor sequences and protein disulfide isomerase. Biochemistry 35, 15547-15557.
15. Hass, G.M. & Ryan, C.A. (1981) Carboxypeptidase inhibitor from potatoes. Methods Enzymol. 80, 778-791.
16. Mas, J.M., Aloy, P., Marti-Renom, M., Blanco-Aparicio, C., Molina, M.A., de Llorens, R., Querol, E. & Aviles, F.X. (1998) Protein similarities beyond disulphide bridge topology. J. Mol. Biol. 284, 541-548.
17. Villanueva, J., Canals, F., Prat, S., Ludevid, D., Querol, E. & Aviles, F.X. (1998) Characterization of the wound-induced metallocarboxypeptidase inhibitor from potatoe: cDNA sequence, induction of gene expression, subcellular immunolocalization and potential roles of the C terminal propeptide. FEBS Lett. 440, 175-182.
18. Chang, J.-Y., Canals, F., Schindler, P., Querol, E. & Aviles, F.X. (1994) The disulfide folding pathway of potato carboxypeptidase inhibitor. J. Biol. Chem. 269, 22087-22090.
19. Chang, J.-Y., Li, L., Canals, F. & Aviles, F.X. (2000) The unfolding pathway and conformational stability of potato carboxypeptidase inhibitor. J. Biol. Chem. 275, 14205-14211.
20. Molina, M.A., Aviles, F.X. & Querol, E. (1992) Expression of a synthetic gene encoding potato carboxypeptidase inhibitor using a bacterial secretion vector. Gene 116, 129-138.
21. Ghrayeb, J., Kimura, H., Takahara, M., Hsiung, H., Masui, Y. & Inouye, M. (1984) Secretion cloning vectors in Escherichia coli. EMBO J. 3, 2437-2442.
22. Venhudová, G., Canals, F., Querol, E. & Aviles, F.X. (2001) Mutations in the N- and C-terminal tails of potato carboxypeptidase inhibitor influence its oxidative refolding process at the reshuffling stage. J. Biol. Chem. 276, 11683-11690.
23. Peranen, J., Rikkonen, M., Hyvonen, M. & Kaariainen, L. (1996) T7 vectors with a modified T7lac promoter for expression of proteins in Escherichia coli. Anal. Biochem. 236, 371-373.
24. Studier, F.W., Rosenberg, A.H., Dunn, J.J. & Dubendorf, J.W. (1990) Use of T7 RNA polimerase to direct expression of cloned genes. Methods Enzymol. 185, 60-89.
25. Chatrenet, B. & Chang, J.-Y. (1993) The disulfide folding pathway of hirudin elucidated by stop/go folding experiments. J. Biol. Chem. 268, 20988-20996.
26. 15N NMR. Proteins 50, 410-422.
27. Villanueva, J., Canals, F., Villegas, V., Querol, E. & Aviles, F.X. (2000) Hydrogen exchange monitored by MALDI-TOF mass spectrometry for rapid characterization of the stability and conformation of proteins. FEBS Lett. 472, 27-33.
28. Villanueva, J., Villegas, V., Querol, E., Aviles, F.X. & Serrano, L. (2002) Protein secondary structure and stability determined by combining exoproteolysis and matrix-assisted laser desorption/ionization time-of-flight mass spectromety. J. Mass. Spec. 37, 974-984.
29. Morel, N. & Massoulie, J. (1997) Expression and processing of vertebrate acetylcholinesterase in the yeast Pichia pastoris. Biochem. J. 328, 121-129.
30. Chaudhary, P.M., Eby, M.T., Jasmin, A. & Hood, L. (1999) Activation of the c-Jun N-terminal kinase/stress-activated protein Kinase pathway by overexpresssion of caspase-8 and its homologs. J. Biol. Chem. 274, 19211-19219.
31. Kim, K.S., Fuchs, J.A. & Woodward, C.K. (1993) Hydrogen exchange identities native-state motional domains important in protein folding. Biochemistry 32, 9600-9608.
32. Woodward, C. (1993) Is the slow exchange core the protein folding core? TIBS 18, 359-360.