pubmed-article:11274393 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:11274393 | lifeskim:mentions | umls-concept:C0043393 | lld:lifeskim |
pubmed-article:11274393 | lifeskim:mentions | umls-concept:C0285558 | lld:lifeskim |
pubmed-article:11274393 | lifeskim:mentions | umls-concept:C1705328 | lld:lifeskim |
pubmed-article:11274393 | lifeskim:mentions | umls-concept:C0812228 | lld:lifeskim |
pubmed-article:11274393 | lifeskim:mentions | umls-concept:C0172982 | lld:lifeskim |
pubmed-article:11274393 | lifeskim:mentions | umls-concept:C1421867 | lld:lifeskim |
pubmed-article:11274393 | lifeskim:mentions | umls-concept:C0439855 | lld:lifeskim |
pubmed-article:11274393 | lifeskim:mentions | umls-concept:C0205360 | lld:lifeskim |
pubmed-article:11274393 | lifeskim:mentions | umls-concept:C1334043 | lld:lifeskim |
pubmed-article:11274393 | pubmed:issue | 7 | lld:pubmed |
pubmed-article:11274393 | pubmed:dateCreated | 2001-3-29 | lld:pubmed |
pubmed-article:11274393 | pubmed:abstractText | 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. | lld:pubmed |
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pubmed-article:11274393 | pubmed:language | eng | lld:pubmed |
pubmed-article:11274393 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11274393 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:11274393 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:11274393 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:11274393 | pubmed:month | Mar | lld:pubmed |
pubmed-article:11274393 | pubmed:issn | 0027-8424 | lld:pubmed |
pubmed-article:11274393 | pubmed:author | pubmed-author:RoseAA | lld:pubmed |
pubmed-article:11274393 | pubmed:author | pubmed-author:GautschiMM | lld:pubmed |
pubmed-article:11274393 | pubmed:author | pubmed-author:RospertSS | lld:pubmed |
pubmed-article:11274393 | pubmed:author | pubmed-author:WUM LML | lld:pubmed |
pubmed-article:11274393 | pubmed:author | pubmed-author:LilieHH | lld:pubmed |
pubmed-article:11274393 | pubmed:author | pubmed-author:LithgowTT | lld:pubmed |
pubmed-article:11274393 | pubmed:author | pubmed-author:RücknagelPP | lld:pubmed |
pubmed-article:11274393 | pubmed:author | pubmed-author:Fünfschilling... | lld:pubmed |
pubmed-article:11274393 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:11274393 | pubmed:day | 27 | lld:pubmed |
pubmed-article:11274393 | pubmed:volume | 98 | lld:pubmed |
pubmed-article:11274393 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:11274393 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:11274393 | pubmed:pagination | 3762-7 | lld:pubmed |
pubmed-article:11274393 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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