Ribosome-associated chaperones as key players in proteostasis

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2012
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Preissler, Steffen
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Trends in Biochemical Sciences. 2012, 37(7), pp. 274-283. ISSN 0968-0004. eISSN 1362-4326. Available under: doi: 10.1016/j.tibs.2012.03.002
Zusammenfassung

De novo protein folding is delicate and error-prone and requires the guidance of molecular chaperones. Besides cytosolic and organelle-specific chaperones, cells have evolved ribosome-associated chaperones that support early folding events and prevent misfolding and aggregation. This class of chaperones includes the bacterial trigger factor (TF), the archaeal and eukaryotic nascent polypeptide-associated complex (NAC) and specialized eukaryotic heat shock protein (Hsp) 70/40 chaperones. This review focuses on the cellular activities of ribosome-associated chaperones and highlights new findings indicating additional functions beyond de novo folding. These activities include the assembly of oligomeric complexes, such as ribosomes, modulation of translation and targeting of proteins.

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570 Biowissenschaften, Biologie
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ISO 690PREISSLER, Steffen, Elke DEUERLING, 2012. Ribosome-associated chaperones as key players in proteostasis. In: Trends in Biochemical Sciences. 2012, 37(7), pp. 274-283. ISSN 0968-0004. eISSN 1362-4326. Available under: doi: 10.1016/j.tibs.2012.03.002
BibTex
@article{Preissler2012-07Ribos-21399,
  year={2012},
  doi={10.1016/j.tibs.2012.03.002},
  title={Ribosome-associated chaperones as key players in proteostasis},
  number={7},
  volume={37},
  issn={0968-0004},
  journal={Trends in Biochemical Sciences},
  pages={274--283},
  author={Preissler, Steffen and Deuerling, Elke}
}
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