Tertiary structure formation in the propeptide of subtilisin BPN' by successive amino acid replacements and its close relation to function

Journal of Molecular Biology

Volumn 277, Issue 5, 1998, Pages 1007-1013

  Kojima, Shuichi ^a   Minagawa, Tetsuya ^a   Miura, Kin Ichiro ^a  

^a GAKUSHUIN UNIVERSITY   (Japan)

Author keywords

Amino acid replacement; Propeptide; Protease inhibitor; Subtilism; Tertiary structure formation

Indexed keywords

ALANINE; CHAPERONE; GLYCINE; ISOLEUCINE; PHENYLALANINE; SUBTILISIN; VALINE;

AMINO ACID SUBSTITUTION; ARTICLE; CIRCULAR DICHROISM; CONTROLLED STUDY; HYDROPHOBICITY; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE;

EID: 0032540306     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1998.1671     Document Type: Article

References (23)

1. Bensadoun A., Weinstein D. Assay of protein in the presence of interfering materials. Anal. Biochem. 70:1976;241-250
2. Bryan P., Wang L., Hoskins J., Ruvinov S., Strausberg S., Alexander P., Almog O., Gilliland G., Gallagher T. Catalysis of a protein folding reaction mechanistic implications of the 2.0 Å structure of the subtilisin-prodomain complex. Biochemistry. 34:1995;10310-10318
3. Dohmae N., Takio K., Tsumuraya Y., Hashimoto Y. The complete amino acid sequences of two serine proteinase inhibitors from the fruiting bodies of a basidiomycete, Pleurotus ostreatus. Arch. Biochem. Biophys. 316:1995;498-506
4. Eder J., Rheinnecker M., Fersht A.R. Folding of subtilisin BPN′ characterization of a folding intermediate. Biochemistry. 32:1993;18-26
5. Eder J., Rheinnecker M., Fersht A.R. Folding of subtilisin BPN′ role of the pro-sequence. J. Mol. Biol. 233:1993;293-304
6. Gallagher T., Gilliland G., Wang L., Bryan P. The prosegment-subtilisin BPN′ complex crystal structure of a specific 'foldase'. Structure. 3:1995;907-914
7. Hu Z., Haghjoo K., Jordan F. Further evidence for the structure of the subtilisin propeptide and its interactions with mature subtilisin. J. Biol. Chem. 271:1996;3375-3384
8. Ikemura H., Takagi H., Inouye M. Requirement of pro-sequence for the production of active subtilisin E in Escherichia coli. J. Biol. Chem. 262:1987;7859-7864
9. Kojima S., Obata S., Kumagai I., Miura K. Alteration of the specificity of the Streptomyces subtilisin inhibitor by gene engineering. Bio/Technology. 8:1990;449-452
10. Kojima S., Kumagai I., Miura K. Requirement for a disulfide bridge near the reactive site of protease inhibitor SSI (Streptomyces subtilisin inhibitor) for its inhibitory action. J. Mol. Biol. 230:1993;395-399
11. Kojima S., Minagawa T., Miura K. The propeptide of subtilisin BPN′ as a temporary inhibitor and effect of an amino acid replacement on its inhibitory activity. FEBS Letters. 411:1997;128-132
12. Li Y., Hu Z., Jordan F., Inouye M. Functional analysis of the propeptide of subtilisin E as an intramolecular chaperone for protein folding. Refolding and inhibitory abilities of propeptide mutants. J. Biol. Chem. 270:1995;25127-25132
13. Maier K., Müller H., Tesch R., Trolp R., Witt I., Holzer H. Primary structure of yeast proteinase B inhibitor 2. J. Biol. Chem. 254:1979;12555-12561
14. Moehle C.M., Tizard R., Lemmon S.K., Smart J., Jones E.W. Protease B of the lysosomelike vacuole of the yeast Saccharomyces cerevisiae is homologous to the subtilisin family of serine proteases. Mol. Cell. Biol. 7:1987;4390-4399
15. Ohta Y., Inouye M. Pro-subtilisin E purification and characterization of its autoprocessing to active subtilisin E in vitro. Mol. Microbiol. 4:1990;295-304
16. Ohta Y., Hojo H., Aimoto S., Kobayashi T., Zhu X., Jordan F., Inouye M. Pro-peptide as an intramolecular chaperone renaturation of denatured subtilisin E with a synthetic pro-peptide. Mol. Microbiol. 5:1991;1507-1510
17. Pakula A.A., Sauer R.T. Reverse hydrophobic effects relieved by amino-acid substitutions at a protein surface. Nature. 344:1990;363-364
18. Ruvinov S., Wang L., Ruan B., Almog O., Gilliland G.L., Eisenstein E., Bryan P.N. Engineering the independent folding of the subtilisin BPN′ prodomain analysis of two-state folding versus protein stability. Biochemistry. 36:1997;10414-10421
19. Shinde U., Inouye M. Intramolecular chaperones and protein folding. Trends Biol. Sci. 18:1993;442-447
20. Shinde U., Inouye M. The structural and functional organization of intramolecualr chaperones the N-terminal propeptides which mediate protein folding. J. Biochem. 115:1994;629-636
21. Shinde U., Li Y., Chatterjee S., Inouye M. Folding pathway mediated by an intramolecular chaperone. Proc. Natl Acad. Sci. USA. 90:1993;6924-6928
22. Strausberg S., Alexander P., Wang L., Schwarz F., Bryan P. Catalysis of a protein folding reaction thermodynamic and kinetic analysis of subtilisin BPN′ interactions with its propeptide fragment. Biochemistry. 32:1993;8112-8119
23. Wang L., Ruvinov S., Strausberg S., Gallagher T., Gilliland G., Bryan P.N. Prodomain mutations at the subtilisin interface correlation of binding energy and the rate of catalyzed folding. Biochemistry. 34:1995;15415-15420