@article{Deuerling1999Trigg-8650,
  year={1999},
  doi={10.1038/23301},
  title={Trigger factor and DnaK cooperate in folding of newly synthesized proteins},
  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}
}

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    <dcterms:title>Trigger factor and DnaK cooperate in folding of newly synthesized proteins</dcterms:title>
    <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:45:23Z</dcterms:available>
    <dc:creator>Deuerling, Elke</dc:creator>
    <dcterms:bibliographicCitation>First publ. in: Nature 400 (1999), pp. 693-696</dcterms:bibliographicCitation>
    <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:45:23Z</dc:date>
    <dc:contributor>Tomoyasu, Toshifumi</dc:contributor>
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    <dc:contributor>Mogk, Axel</dc:contributor>
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    <dc:creator>Tomoyasu, Toshifumi</dc:creator>
    <dc:creator>Mogk, Axel</dc:creator>
    <dc:contributor>Schulze-Specking, Agnes</dc:contributor>
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    <dcterms:issued>1999</dcterms:issued>
    <dc:contributor>Bukau, Bernd</dc:contributor>
    <dc:creator>Bukau, Bernd</dc:creator>
    <dc:contributor>Deuerling, Elke</dc:contributor>
    <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>
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    <dc:creator>Schulze-Specking, Agnes</dc:creator>
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