Promiscuous Substrate Recognition in Folding and Assembly Activities of the Trigger Factor Chaperone

@article{MartinezHackert2009PromiscuousSR,
  title={Promiscuous Substrate Recognition in Folding and Assembly Activities of the Trigger Factor Chaperone},
  author={Erik Martinez-Hackert and Wayne A. Hendrickson},
  journal={Cell},
  year={2009},
  volume={138},
  pages={923-934}
}
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… CONTINUE READING
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