@article{Fiaux2010Struc-7641,
  year={2010},
  doi={10.1074/jbc.M109.075804},
  title={Structural Analysis of the Ribosome-associated Complex (RAC) Reveals an Unusual Hsp70/Hsp40 Interaction},
  number={5},
  volume={285},
  issn={0021-9258},
  journal={The Journal of Biological Chemistry},
  pages={3227--3234},
  author={Fiaux, Jocelyne and Horst, Janina and Scior, Annika and Preissler, Steffen and Koplin, Ansgar and Bukau, Bernd and Deuerling, Elke}
}

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    <dcterms:bibliographicCitation>First publ. in: The Journal of Biological Chemistry 285 (2010), 5, pp. 3227-3234</dcterms:bibliographicCitation>
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    <dc:creator>Bukau, Bernd</dc:creator>
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    <dc:contributor>Fiaux, Jocelyne</dc:contributor>
    <dc:contributor>Preissler, Steffen</dc:contributor>
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    <dc:contributor>Koplin, Ansgar</dc:contributor>
    <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:36:00Z</dc:date>
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    <dc:contributor>Deuerling, Elke</dc:contributor>
    <dc:creator>Scior, Annika</dc:creator>
    <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:36:00Z</dcterms:available>
    <dc:contributor>Bukau, Bernd</dc:contributor>
    <dcterms:title>Structural Analysis of the Ribosome-associated Complex (RAC) Reveals an Unusual Hsp70/Hsp40 Interaction</dcterms:title>
    <dcterms:issued>2010</dcterms:issued>
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    <dc:creator>Koplin, Ansgar</dc:creator>
    <dc:creator>Preissler, Steffen</dc:creator>
    <dc:contributor>Scior, Annika</dc:contributor>
    <dc:creator>Deuerling, Elke</dc:creator>
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    <dcterms:abstract xml:lang="eng">Yeast Zuotin and Ssz are members of the conserved Hsp40 and Hsp70 chaperone families, respectively, but compared with canonical homologs, they atypically form a stable heterodimer termed ribosome-associated complex (RAC). RAC acts as co-chaperone for another Hsp70 to assist de novo protein folding. In this study, we identified the molecular basis for the unusual Hsp70/Hsp40 pairing using amide hydrogen exchange (HX) coupled with mass spectrometry and mutational analysis. Association of Ssz with Zuotin strongly decreased the conformational dynamics mainly in the C-terminal domain of Ssz, whereas Zuotin acquired strong conformational stabilization in its N-terminal segment. Deletion of the highly flexible N terminus of Zuotin abolished stable association with Ssz in vitro and caused a phenotype resembling the loss of Ssz function in vivo. Thus, the C-terminal domain of Ssz, the N-terminal extension of Zuotin, and their mutual stabilization are the major structural determinants for RAC assembly. We furthermore found dynamic changes in the J-domain of Zuotin upon complex formation that might be crucial for RAC co-chaperone function. Taken together, we present a novel mechanism for converting Zuotin and Ssz chaperones into a functionally active dimer.</dcterms:abstract>
    <dc:contributor>Horst, Janina</dc:contributor>
    <dc:creator>Horst, Janina</dc:creator>
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    <dc:creator>Fiaux, Jocelyne</dc:creator>
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