@article{Hesterkamp1997amino-7043,
  year={1997},
  doi={10.1074/jbc.272.35.21865},
  title={The amino-terminal 118 amino acids of Escherichia coli trigger factor constitute a domain that is necessary and sufficient for binding to ribosomes},
  number={35},
  volume={272},
  issn={0021-9258},
  journal={Journal of Biological Chemistry},
  pages={21865--21871},
  author={Hesterkamp, Thomas and Deuerling, Elke and Bukau, Bernd}
}

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    <dcterms:title>The amino-terminal 118 amino acids of Escherichia coli trigger factor constitute a domain that is necessary and sufficient for binding to ribosomes</dcterms:title>
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    <dcterms:issued>1997</dcterms:issued>
    <dc:language>eng</dc:language>
    <dc:creator>Hesterkamp, Thomas</dc:creator>
    <dcterms:bibliographicCitation>First publ. in: Journal of Biological Chemistry 272 (1997), 35, pp. 21865 21871</dcterms:bibliographicCitation>
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    <dc:creator>Bukau, Bernd</dc:creator>
    <dc:contributor>Hesterkamp, Thomas</dc:contributor>
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    <dc:contributor>Bukau, Bernd</dc:contributor>
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    <dcterms:abstract xml:lang="eng">Escherichia coli trigger factor has prolyl-isomerase and chaperone activities and associates with nascent polypeptide chains. Trigger factor has a binding site on ribosomes, which is a prerequisite for its efficient association with nascent chains and its proposed function as a cotranslational folding catalyst. We set out to identify the domain of trigger factor that mediates ribosome binding. Of a series of recombinant fragments, the amino-terminal fragments, TF (1 144) and TF (1 247), cofractionated with ribosomes from cell extracts and rebound to isolated ribosomes in vitro. They competed efficiently with full-length trigger factor for stoichiometric binding to a single site on the large ribosomal subunit. However, TF (1 144) and TF (1 247) differed from full-length trigger factor in that their association with ribosomes was not strengthened by the presence of nascent chains, indicating a role for carboxyl-terminal trigger factor segment in sensing the translational status. The domain responsible for ribosome binding was further investigated by limited proteolysis of recombinant fragments. A stable domain comprising the aminoterminal 118 residues was identified that was still capable of ribosome binding and thus represents a novel structural and functional element of trigger factor.</dcterms:abstract>
    <dc:creator>Deuerling, Elke</dc:creator>
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    <dc:contributor>Deuerling, Elke</dc:contributor>
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