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Article

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

The Journal of biological chemistry - 11 Nov 1994

Gordon C L, Sather S K, Casjens S, King J

Abstract excerpt

The in vivo conformational substrates of the GroE chaperonins have been difficult to identify, in part because of limited information on in vivo polypeptide chain folding pathways. Temperature-sensitive folding (tsf) mutants have been characterized for the coat protein and tailspike protein of phage P22. These mutations block intracellular folding at restrictive temperature by increasing the lability of folding...

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PMID: 7961726

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Research trail→

Click a neighbor to travelStep 1 · 12 closest

Selective in vivo rescue by GroEL/ES of thermolabile folding intermediates to phage P22 structural proteins.PMID 7961726Read ↗

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

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

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

Prevalence of temperature sensitive folding mutations in the parallel beta coil domain of the phage P22 tailspike endorhamnosidase.Semantic proximity Read ↗

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

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

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

Isolation of suppressors of temperature-sensitive folding mutations.Semantic proximity Read ↗

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

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