Ribosome-tethered molecular chaperones

The first line of defense against protein misfolding?

Elizabeth A. Craig, Helene C. Eisenman, Heather Hundley

Research output: Contribution to journalArticle

61 Citations (Scopus)

Abstract

Folding of many cellular proteins is facilitated by molecular chaperones. Analysis of both prokaryotic and lower eukaryotic model systems has revealed the presence of ribosome-associated molecular chaperones, thought to be the first line of defense against protein aggregation as translating polypeptides emerge from the ribosome. However, structurally unrelated chaperones have evolved to carry out these functions in different microbes. In the yeast Saccharomyces cerevisiae, an unusual complex of Hsp70 and J-type chaperones associates with ribosome-bound nascent chains, whereas in Escherichia coli the ribosome-associated peptidyl-prolyl-cis-trans isomerase, trigger factor, plays a predominant role.

Original languageEnglish (US)
Pages (from-to)157-162
Number of pages6
JournalCurrent Opinion in Microbiology
Volume6
Issue number2
DOIs
StatePublished - Apr 2003
Externally publishedYes

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Molecular Chaperones
Ribosomes
Proteins
Peptidylprolyl Isomerase
Saccharomyces cerevisiae
Yeasts
Escherichia coli
Peptides

ASJC Scopus subject areas

  • Infectious Diseases
  • Microbiology

Cite this

Ribosome-tethered molecular chaperones : The first line of defense against protein misfolding? / Craig, Elizabeth A.; Eisenman, Helene C.; Hundley, Heather.

In: Current Opinion in Microbiology, Vol. 6, No. 2, 04.2003, p. 157-162.

Research output: Contribution to journalArticle

Craig, Elizabeth A. ; Eisenman, Helene C. ; Hundley, Heather. / Ribosome-tethered molecular chaperones : The first line of defense against protein misfolding?. In: Current Opinion in Microbiology. 2003 ; Vol. 6, No. 2. pp. 157-162.
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