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Article

A concerted mechanism for the suppression of a folding defect through interactions with chaperones.

The Journal of biological chemistry - 23 Apr 2004

Doyle Shannon M, Anderson Eric, Parent Kristin N, Teschke Carolyn M

Abstract excerpt

Specific amino acid substitutions confer a temperature-sensitive-folding (tsf) phenotype to bacteriophage P22 coat protein. Additional amino acid substitutions, called suppressor substitutions (su), relieve the tsf phenotype. These su substitutions are proposed to increase the efficiency of procapsid assembly, favoring correct folding over improper aggregation. Our recent studies indicate that the molecular...

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Identifiers

PMID: 14764588
DOI: 10.1074/jbc.M400467200

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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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Research trail→

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A concerted mechanism for the suppression of a folding defect through interactions with chaperones.PMID 14764588Read ↗

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

Global suppression of protein folding defects and inclusion body formation.Semantic proximity Read ↗

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

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

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

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

Genetic properties of temperature-sensitive folding mutants of the coat protein of phage P22.Semantic proximity Read ↗

A tail of protein folding.Semantic proximity Read ↗

First-step mutations for adaptation at elevated temperature increase capsid stability in a virus.Semantic proximity Read ↗

Invivo folding efficiencies for mutants of the P22 tailspike beta-helix protein correlate with predicted stability changes.Semantic proximity Read ↗

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

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