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PMID: 6954486 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

Trimeric intermediate in the in vivo folding and subunit assembly of the tail spike endorhamnosidase of bacteriophage P22.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 79 ·No. 11 ·1982-06-00 ·Pages 3403-7

Goldenberg D, King J

Abstract

Newly synthesized tail spike polypeptide chains mature from trypsin- and NaDodSO4-sensitive unfolded chains to trypsin- and NaDodSO4-resistant native trimers with a t1/2 of 5 min at 30 degrees C. A metastable intermediate in subunit folding and assembly was trapped by chilling and isolated by electrophoresis through nondenaturing gels in the cold. A fraction of the intermediate could be matured into native trimers in vitro by incubating at physiological temperature. Mixing experiments with electrophoretically distinct mutant proteins showed that the precursor that matured in vitro represented three tail spike polypeptide chains already associated with each other but not fully folded. Identification of this intermediate reveals that the processes of polypeptide chain folding and subunit assembly are coupled in this large structural protein.

MeSH Terms
Electrophoresis, Polyacrylamide Gel/methods Glycoside Hydrolases/biosynthesis Macromolecular Substances Protein Conformation Salmonella Phages/enzymology,ultrastructure Virus Replication
Chemicals
Macromolecular Substances Glycoside Hydrolases alpha-L-rhamnosidase
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Goldenberg D
King J
References (30)
30 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.79.11.3403
Published
1982-06-00
Pages
3403-7
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC346428
Subset
IM
Grants
NIGMS NIH HHS · GM17,980 · United States
External Links
PubMed source DOI: 10.1073/pnas.79.11.3403 PMC Full Text View journal details
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