The Crystal Structure of Archaeal Nascent Polypeptide-associated Complex (NAC) Reveals a Unique Fold and the Presence of a Ubiquitin-associated Domain-Reference-Cited by-同舟云学术

The Crystal Structure of Archaeal Nascent Polypeptide-associated Complex (NAC) Reveals a Unique Fold and the Presence of a Ubiquitin-associated Domain

Published:2005-04 Issue:16 Volume:280 Page:15849-15854
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Spreter Thomas,Pech Markus,Beatrix Birgitta

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference47 articles.

1. Unregulated exposure of the ribosomal M-site caused by NAC depletion results in delivery of non-secretory polypeptides to the Sec61 complex

2. A protein complex required for signal-sequence-specific sorting and translocation

3. NAC covers ribosome-associated nascent chains thereby forming a protective environment for regions of nascent chains just emerging from the peptidyl transferase center.

4. The intrinsic ability of ribosomes to bind to endoplasmic reticulum membranes is regulated by signal recognition particle and nascent-polypeptide-associated complex.

5. Nascent polypeptide-associated complex protein prevents mistargeting of nascent chains to the endoplasmic reticulum.

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