Trigger factor and DnaK cooperate in folding of newly synthesized proteins

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DEUERLING, Elke, Agnes SCHULZE-SPECKING, Toshifumi TOMOYASU, Axel MOGK, Bernd BUKAU, 1999. Trigger factor and DnaK cooperate in folding of newly synthesized proteins. In: Nature. 400(6745), pp. 693-696. ISSN 0028-0836

@article{Deuerling1999Trigg-8650, title={Trigger factor and DnaK cooperate in folding of newly synthesized proteins}, year={1999}, doi={10.1038/23301}, number={6745}, volume={400}, issn={0028-0836}, journal={Nature}, pages={693--696}, author={Deuerling, Elke and Schulze-Specking, Agnes and Tomoyasu, Toshifumi and Mogk, Axel and Bukau, Bernd} }

<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/123456789/8650"> <dc:contributor>Bukau, Bernd</dc:contributor> <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:45:23Z</dcterms:available> <dc:format>application/pdf</dc:format> <dc:creator>Deuerling, Elke</dc:creator> <dcterms:abstract xml:lang="eng">The role of molecular chaperones in assisting the folding of newly synthesized proteins in the cytosol is poorly understood. In Escherichia coli, GroEL assists folding of only a minority of proteins1 and the Hsp70 homologue DnaK is not essential for protein folding or cell viability at intermediate growth temperatures. The major protein associated with nascent polypeptides is ribosome-bound trigger factor which displays chaperone and prolyl isomerase activities in vitro. Here we show that Δtig::kan mutants lacking trigger factor have no defects in growth or protein folding. However, combined Δtig::kan and ΔdnaK mutations cause synthetic lethality. Depletion of DnaK in the Δtig::kan mutant results in massive aggregation of cytosolic proteins. In Δtig::kan cells, an increased amount of newly synthesized proteins associated transiently with DnaK. These findings show in vivo activity for a ribosome-associated chaperone, trigger factor, in general protein folding, and functional cooperation of this protein with a cytosolic Hsp70. Trigger factor and DnaK cooperate to promote proper folding of a variety of E. coli proteins, but neither is essential for folding and viability at intermediate growth temperatures.</dcterms:abstract> <dc:language>eng</dc:language> <dc:creator>Tomoyasu, Toshifumi</dc:creator> <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/8650"/> <dc:contributor>Deuerling, Elke</dc:contributor> <dcterms:rights rdf:resource="https://creativecommons.org/licenses/by-nc-nd/2.0/legalcode"/> <dc:rights>deposit-license</dc:rights> <dc:creator>Bukau, Bernd</dc:creator> <dc:creator>Schulze-Specking, Agnes</dc:creator> <dc:creator>Mogk, Axel</dc:creator> <dcterms:issued>1999</dcterms:issued> <dcterms:bibliographicCitation>First publ. in: Nature 400 (1999), pp. 693-696</dcterms:bibliographicCitation> <dc:contributor>Tomoyasu, Toshifumi</dc:contributor> <dcterms:title>Trigger factor and DnaK cooperate in folding of newly synthesized proteins</dcterms:title> <dc:contributor>Schulze-Specking, Agnes</dc:contributor> <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:45:23Z</dc:date> <dc:contributor>Mogk, Axel</dc:contributor> </rdf:Description> </rdf:RDF>

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