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PMID:19737520

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Citation

Martinez-Hackert, E and Hendrickson, WA (2009) Promiscuous substrate recognition in folding and assembly activities of the trigger factor chaperone. Cell 138:923-34

Abstract

Trigger factor (TF) is a molecular chaperone that binds to bacterial ribosomes where it contacts emerging nascent chains, but TF is also abundant free in the cytosol where its activity is less well characterized. In vitro studies show that TF promotes protein refolding. We find here that ribosome-free TF stably associates with and rescues from misfolding a large repertoire of full-length proteins. We identify over 170 members of this cytosolic Escherichia coli TF substrate proteome, including ribosomal protein S7. We analyzed the biochemical properties of a TF:S7 complex from Thermotoga maritima and determined its crystal structure. Thereby, we obtained an atomic-level picture of a promiscuous chaperone in complex with a physiological substrate protein. The structure of the complex reveals the molecular basis of substrate recognition by TF, indicates how TF could accelerate protein folding, and suggests a role for TF in the biogenesis of protein complexes.

Links

PubMed PMC2799252 Online version:10.1016/j.cell.2009.07.044

Keywords

Bacterial Proteins/chemistry; Bacterial Proteins/metabolism; Crystallography, X-Ray; Escherichia coli/metabolism; Escherichia coli Proteins/chemistry; Models, Molecular; Molecular Chaperones/chemistry; Peptidylprolyl Isomerase/chemistry; Protein Folding; Proteome/analysis; Ribosomal Proteins/metabolism; Thermotoga maritima/metabolism

Significance

Annotations

Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status

ECOLI:RS7

enables

GO:0005515: protein binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:P0A850

F

Seeded From UniProt

complete

ECOLI:RL28

enables

GO:0005515: protein binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:P0A850

F

Seeded From UniProt

complete

ECOLI:TIG

enables

GO:0005515: protein binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:P02359

F

Seeded From UniProt

complete

ECOLI:TIG

enables

GO:0005515: protein binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:P0A7M2

F

Seeded From UniProt

complete

ECOLI:TIG

enables

GO:0005515: protein binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:P0A910

F

Seeded From UniProt

complete

ECOLI:OMPA

enables

GO:0005515: protein binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:P0A850

F

Seeded From UniProt

complete

THEMA:RS7

enables

GO:0005515: protein binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:Q9WZF8

F

Seeded From UniProt

complete

THEMA:TIG

enables

GO:0005515: protein binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:P38526

F

Seeded From UniProt

complete


See also

References

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