@article{Merz2006Cterm-7046,
  year={2006},
  title={The C-terminal domain of Escherichia coli trigger factor represents the central module of its chaperone activity},
  number={42},
  volume={281},
  issn={0021-9258},
  journal={Journal of Biological Chemistry},
  pages={31963--31971},
  author={Merz, Frieder and Hoffmann, Anja and Rutkowska, Anna and Zachmann-Brand, Beate and Bukau, Bernd and Deuerling, Elke}
}

<rdf:RDF
    xmlns:dcterms="http://purl.org/dc/terms/"
    xmlns:dc="http://purl.org/dc/elements/1.1/"
    xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#"
    xmlns:bibo="http://purl.org/ontology/bibo/"
    xmlns:dspace="http://digital-repositories.org/ontologies/dspace/0.1.0#"
    xmlns:foaf="http://xmlns.com/foaf/0.1/"
    xmlns:void="http://rdfs.org/ns/void#"
    xmlns:xsd="http://www.w3.org/2001/XMLSchema#" > 
  <rdf:Description rdf:about="https://kops.uni-konstanz.de/server/rdf/resource/123456789/7046">
    <dc:contributor>Merz, Frieder</dc:contributor>
    <foaf:homepage rdf:resource="http://localhost:8080/"/>
    <dcterms:title>The C-terminal domain of Escherichia coli trigger factor represents the central module of its chaperone activity</dcterms:title>
    <void:sparqlEndpoint rdf:resource="http://localhost/fuseki/dspace/sparql"/>
    <dc:language>eng</dc:language>
    <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:31:05Z</dcterms:available>
    <dc:creator>Deuerling, Elke</dc:creator>
    <dc:rights>Attribution-NonCommercial-NoDerivs 2.0 Generic</dc:rights>
    <dcterms:bibliographicCitation>First publ. in: Journal of Biological Chemistry 281 (2006), 42, pp. 31963 31971</dcterms:bibliographicCitation>
    <dc:creator>Rutkowska, Anna</dc:creator>
    <dc:creator>Merz, Frieder</dc:creator>
    <dspace:isPartOfCollection rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/28"/>
    <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:31:05Z</dc:date>
    <dcterms:hasPart rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/7046/1/The_C_terminal_Domain_of_Escherichia_coli_Trigger_Factor.pdf"/>
    <dcterms:rights rdf:resource="http://creativecommons.org/licenses/by-nc-nd/2.0/"/>
    <dcterms:issued>2006</dcterms:issued>
    <dc:contributor>Hoffmann, Anja</dc:contributor>
    <dc:creator>Hoffmann, Anja</dc:creator>
    <dc:contributor>Rutkowska, Anna</dc:contributor>
    <dc:creator>Bukau, Bernd</dc:creator>
    <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/7046"/>
    <dc:contributor>Deuerling, Elke</dc:contributor>
    <dcterms:isPartOf rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/28"/>
    <dc:contributor>Bukau, Bernd</dc:contributor>
    <dc:contributor>Zachmann-Brand, Beate</dc:contributor>
    <dc:creator>Zachmann-Brand, Beate</dc:creator>
    <dc:format>application/pdf</dc:format>
    <dcterms:abstract xml:lang="eng">In bacteria, ribosome-bound Trigger Factor assists the folding of newly synthesized proteins. The N-terminal domain (N) of Trigger Factor mediates ribosome binding, whereas the middle domain (P) harbors peptidyl-prolyl isomerase activity. The function of the C-terminal domain (C) has remained enigmatic due to structural instability in isolation. Here, we have characterized a stabilized version of theCdomain (CS), designed on the basis of the recently solved atomic structure of Trigger Factor. Strikingly, only the isolated CS domain or domain combinations thereof (NCS, PCS) revealed substantial chaperone activity in vitro and in vivo. Furthermore, to disrupt the C domain without affecting the overall Trigger Factor structure, we generated a mutant (Δ53) by deletion of the C-terminal 53 amino acid residues. This truncation caused the complete loss of the chaperone activity of Trigger Factor in vitro and severely impaired its function in vivo. Therefore, we conclude that the chaperone activity of Trigger Factor critically depends on its C-terminal domain as the central structural chaperone module. Intriguingly, a structurally similar module is found in the periplasmic chaperone SurA and in MPN555, a protein of unknown function. We speculate that this conserved module can exist solely or in combination with additional domains to fulfill diverse chaperone functions in the cell.</dcterms:abstract>
    <dspace:hasBitstream rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/7046/1/The_C_terminal_Domain_of_Escherichia_coli_Trigger_Factor.pdf"/>
  </rdf:Description>
</rdf:RDF>