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Nascent-polypeptide-associated complex (NAC) is a heterodimeric complex which can reversibly bind to eukaryotic ribosomes. NAC is located in direct proximity to newly synthesized polypeptide chains as they emerge from the ribosome. Although its function is thought to be conserved from yeast to humans our current knowledge about what NAC actually does in a living cell is incomplete. It has been suggested that NAC is a (i) dynamic component of the ribosomal exit tunnel, providing a shield for nascent polypeptides, (ii) negative regulator of translocation into the endoplasmic reticulum and (iii) positive regulator of translocation into the mitochondria. However, none of these hypotheses is generally accepted. Moreover, the individual subunits of NAC have been implicated in processes related to transcription rather than translation, and it is currently under debate whether NAC might be a protein of dual function. This review attempts to summarize the data from different fields and to discuss the partly controversial results in a common context.
- Nascent-polypeptide-associated complex
Cellular and Molecular Life Sciences CMLS
Volume 59, Issue 10 , pp 1632-1639
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- Birkhäuser Verlag
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- Key words. ER translocation; translational repression; bicaudal; chaperone; nascent polypeptide.
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- Author Affiliations
- A1. Max Planck Research Unit for Enzymology of Protein Folding, Weinbergweg 22, 06120 Halle (Germany), DE
- A2. Bristol-Myers Squibb, Pharmaceutical Research Institute, H13-03 P.O. Box 4000, Princeton, New Jersey 08543-4000 (USA), e-mail: email@example.com, US