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Structural Analysis of the Ribosome-associated Complex (RAC) Reveals an Unusual Hsp70/Hsp40 Interaction

Structural Analysis of the Ribosome-associated Complex (RAC) Reveals an Unusual Hsp70/Hsp40 Interaction

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FIAUX, Jocelyne, Janina HORST, Annika SCIOR, Steffen PREISSLER, Ansgar KOPLIN, Bernd BUKAU, Elke DEUERLING, 2010. Structural Analysis of the Ribosome-associated Complex (RAC) Reveals an Unusual Hsp70/Hsp40 Interaction. In: The Journal of Biological Chemistry. 285(5), pp. 3227-3234. ISSN 0021-9258. eISSN 1083-351X

@article{Fiaux2010Struc-7641, title={Structural Analysis of the Ribosome-associated Complex (RAC) Reveals an Unusual Hsp70/Hsp40 Interaction}, year={2010}, doi={10.1074/jbc.M109.075804}, 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} }

<rdf:RDF xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" xmlns:bibo="http://purl.org/ontology/bibo/" xmlns:dc="http://purl.org/dc/elements/1.1/" xmlns:dcterms="http://purl.org/dc/terms/" xmlns:xsd="http://www.w3.org/2001/XMLSchema#" > <rdf:Description rdf:about="https://kops.uni-konstanz.de/rdf/resource/123456789/7641"> <dcterms:bibliographicCitation>First publ. in: The Journal of Biological Chemistry 285 (2010), 5, pp. 3227-3234</dcterms:bibliographicCitation> <dc:creator>Preissler, Steffen</dc:creator> <dc:contributor>Bukau, Bernd</dc:contributor> <dc:creator>Koplin, Ansgar</dc:creator> <dc:contributor>Koplin, Ansgar</dc:contributor> <dc:creator>Horst, Janina</dc:creator> <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:36:00Z</dc:date> <dc:contributor>Scior, Annika</dc:contributor> <dcterms:issued>2010</dcterms:issued> <dc:creator>Deuerling, Elke</dc:creator> <dcterms:rights rdf:resource="http://nbn-resolving.org/urn:nbn:de:bsz:352-20140905103416863-3868037-7"/> <dc:creator>Scior, Annika</dc:creator> <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/7641"/> <dc:contributor>Preissler, Steffen</dc:contributor> <dc:creator>Fiaux, Jocelyne</dc:creator> <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:36:00Z</dcterms:available> <dc:format>application/pdf</dc:format> <dc:contributor>Fiaux, Jocelyne</dc:contributor> <dcterms:title>Structural Analysis of the Ribosome-associated Complex (RAC) Reveals an Unusual Hsp70/Hsp40 Interaction</dcterms:title> <dc:language>eng</dc:language> <dc:rights>deposit-license</dc:rights> <dc:creator>Bukau, Bernd</dc:creator> <dc:contributor>Horst, Janina</dc:contributor> <dc:contributor>Deuerling, Elke</dc:contributor> <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> </rdf:Description> </rdf:RDF>

Dateiabrufe seit 01.10.2014 (Informationen über die Zugriffsstatistik)

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