Cited by 344Protein Structure and DynamicsProtein purification and stabilityEnzyme Structure and Function

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Pro-sequence of subtilisin can guide the refolding of denatured subtilisin in an intermolecular process.

Zhu, Xueli, Ohta, Yoshiji, Jordan, Frank, Inouye, Masayori·1989·Nature

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Abstract

Subtilisin E, an alkaline serine protease consisting of a single polypeptide chain of 275 amino acids is produced from a pre-pro-protein. The pre-sequence functions as the signal peptide for protein secretion across the membrane. Deletion of the pro-sequence yields mature but inactive subtilisin: the 77-amino acid pro-sequence must precede the mature subtilisin to guide the latter into an active conformation. Pro-subtilisin denatured in 6 M guanidine-HCl can be self-processed to the active enzyme intramolecularly, with concomitant cleavage of the pro-sequence, when dialysed against renaturing buffer. We have constructed an active-centre mutant of pro-subtilisin (Asp 32----Asn) which is not processed to active enzyme, unlike the wild-type pro-subtilisin, because intramolecular processing is prevented. Here we report an intermolecular pathway for the refolding of the inactive mature protein to an active enzyme in vitro with the aid of exogenously added pro-sequence. We establish conditions under which the mature inactive form, as well as acid-denatured subtilisins Carlsberg and BPN', can be renatured by the mutant pro-subtilisin.

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Authors: Zhu, X., Ohta, Y., Jordan, F., & Inouye, M.
Affiliations: Rutgers, The State University of New Jersey (US)
ORCID: Jordan, Frank
Inouye, Masayori
Venue: Nature
Publisher: Springer Science and Business Media LLC
Published: 1989-06
Volume: 339
Issue: 6224
Pages: 483-484
ISSN: 0028-0836 (ISSN-L)
1476-4687
DOI: 10.1038/339483a0
OpenAlex: W2045786862
Cited by: 344
References: 10
Citations by year: 2025: 2 · 2024: 2 · 2023: 4 · 2022: 3 · 2021: 2 · 2020: 4 · 2019: 2 · 2018: 3 · 2017: 3 · 2016: 3 · 2015: 5 · 2014: 8 · 2013: 4 · 2012: 10
FWCI: 8.12
Type: journal article
Language: en
Open access: closed
Licence: www.springer.com/tdm (tdm)
Locations: Nature (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein purification and stability
Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
Keywords: subtilisin, protein refolding, protein denaturation, guanidine hydrochloride denaturation, serine protease activation, active site mutants, subtilisin Carlsberg, subtilisin BPN', renaturation
MeSH terms: Enzyme Activation, Enzyme Precursors, Escherichia coli, Genetic Vectors, Kinetics, Peptide Fragments, Plasmids, Protein Conformation, Protein Denaturation, Recombinant Proteins, Subtilisins

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Pro-sequence of subtilisin can guide the refolding of denatured subtilisin in an intermolecular process.

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