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 Delta ssz1 strain, whereas overexpression of Ssz1p did not affect the Delta zuo1 strain, suggesting a pivotal function for the DnaJ homolog.
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| Gene/Complex | Qualifier | Gene Ontology Term | Annotation Extension | Evidence | Source | Assigned On |
|---|---|---|---|---|---|---|
| Ribosome-associated complex | enables | unfolded protein binding | IDA | ComplexPortal | 2014-10-16 | |
| Ribosome-associated complex | enables | ribosome binding | IPI | ComplexPortal | 2014-10-16 | |
| Ribosome-associated complex | involved in | protein folding | BSR | ComplexPortal | 2014-10-16 | |
| Ribosome-associated complex | involved in | 'de novo' cotranslational protein folding | IDA | ComplexPortal | 2014-10-16 | |
| ZUO1 | involved in | 'de novo' cotranslational protein folding | IMP | SGD | 2017-03-10 | |
| SSZ1 | involved in | 'de novo' cotranslational protein folding | IMP | SGD | 2017-03-10 |
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| Evidence ID | Analyze ID | Interactor | Interactor Systematic Name | Interactor | Interactor Systematic Name | Allele | Assay | Annotation | Action | Phenotype | SGA score | P-value | Source | Reference | Note |
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