RAC, A Stable Ribosome-Associated Complex in Yeast Formed by the DnaK-DnaJ Homologs Ssz1p and Zuotin
The yeast cytosol contains multiple homologs of the DnaK and DnaJ chaperone family. Our current understanding of which homologs functionally interact is incomplete. Zuotin is a DnaJ homolog bound to the yeast ribosome. We have now identified the DnaK homolog Ssz1p/Pdr13p as zuotin's partner cha...
Saved in:
Published in: | Proceedings of the National Academy of Sciences - PNAS Vol. 98; no. 7; pp. 3762 - 3767 |
---|---|
Main Authors: | , , , , , , , |
Format: | Journal Article |
Language: | English |
Published: |
United States
National Academy of Sciences
27-03-2001
National Acad Sciences The National Academy of Sciences |
Subjects: | |
Online Access: | Get full text |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
Summary: | The yeast cytosol contains multiple homologs of the DnaK and DnaJ chaperone family. Our current understanding of which homologs functionally interact is incomplete. Zuotin is a DnaJ homolog bound to the yeast ribosome. We have now identified the DnaK homolog Ssz1p/Pdr13p as zuotin's partner chaperone. Zuotin and Ssz1p form a ribosome-associated complex (RAC) that is bound to the ribosome via the zuotin subunit. RAC is unique among the eukaryotic DnaK-DnaJ systems, as the 1:1 complex is stable, even in the presence of ATP or ADP. In vitro, RAC stimulates the translocation of a ribosome-bound mitochondrial precursor protein into mitochondria, providing evidence for its chaperone-like effect on nascent chains. In agreement with the existence of a functional complex, deletion of each RAC subunit resulted in a similar phenotype in vivo. However, overexpression of zuotin partly rescued the growth defect of the Δssz1 strain, whereas overexpression of Ssz1p did not affect the Δzuo1 strain, suggesting a pivotal function for the DnaJ homolog. |
---|---|
Bibliography: | ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 23 ObjectType-Article-1 ObjectType-Feature-2 Communicated by Gottfried Schatz, University of Basel, Reinach, Switzerland To whom reprint requests should be addressed. E-mail: rospert@enzyme-halle.mpg.de. |
ISSN: | 0027-8424 1091-6490 |
DOI: | 10.1073/pnas.071057198 |