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Article

GroEL and GroES control of substrate flux in the in vivo folding pathway of phage P22 coat protein.

The Journal of biological chemistry - 16 Oct 1998

Nakonechny W S, Teschke C M

Abstract excerpt

Our present understanding of the action of the chaperonins GroEL/S on protein folding is based primarily on in vitro studies, whereas the folding of proteins in the cellular milieu has not been as thoroughly investigated. We have developed a means of examining in vivo protein folding and assembly that utilizes the coat protein of bacteriophage P22, a naturally occurring substrate of GroEL/S. Here we show that...

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Identifiers

PMID: 9765246
DOI: 10.1074/jbc.273.42.27236

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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GroEL and GroES control of substrate flux in the in vivo folding pathway of phage P22 coat protein.PMID 9765246Read ↗

Selective in vivo rescue by GroEL/ES of thermolabile folding intermediates to phage P22 structural proteins.Semantic proximity Read ↗

GroEL binds a late folding intermediate of phage P22 coat protein.Semantic proximity Read ↗

In vitro folding of phage P22 coat protein with amino acid substitutions that confer in vivo temperature sensitivity.Semantic proximity Read ↗

Single amino acid substitutions globally suppress the folding defects of temperature-sensitive folding mutants of phage P22 coat protein.Semantic proximity Read ↗

The folded conformation of phage P22 coat protein is affected by amino acid substitutions that lead to a cold-sensitive phenotype.Semantic proximity Read ↗

A concerted mechanism for the suppression of a folding defect through interactions with chaperones.Semantic proximity Read ↗

Aggregation and assembly of phage P22 temperature-sensitive coat protein mutants in vitro mimic the in vivo phenotype.Semantic proximity Read ↗

Stability of wild-type and temperature-sensitive protein subunits of the phage P22 capsid.Semantic proximity Read ↗

Alleviation of a defect in protein folding by increasing the rate of subunit assembly.Semantic proximity Read ↗

Protein folding in the cytoplasm of Escherichia coli: requirements for the DnaK-DnaJ-GrpE and GroEL-GroES molecular chaperone machines.Semantic proximity Read ↗

Proteome-wide analysis of chaperonin-dependent protein folding in Escherichia coli.Semantic proximity Read ↗

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