Publikation:

Trigger factor and DnaK cooperate in folding of newly synthesized proteins

Lade...
Vorschaubild

Datum

1999

Autor:innen

Schulze-Specking, Agnes
Tomoyasu, Toshifumi
Mogk, Axel
Bukau, Bernd

Herausgeber:innen

Kontakt

ISSN der Zeitschrift

Electronic ISSN

ISBN

Bibliografische Daten

Verlag

Schriftenreihe

Auflagebezeichnung

DOI (zitierfähiger Link)
ArXiv-ID

Internationale Patentnummer

Angaben zur Forschungsförderung

Projekt

Open Access-Veröffentlichung
Open Access Green
Core Facility der Universität Konstanz

Gesperrt bis

Titel in einer weiteren Sprache

Publikationstyp
Zeitschriftenartikel
Publikationsstatus
Published

Erschienen in

Nature. 1999, 400(6745), pp. 693-696. ISSN 0028-0836. Available under: doi: 10.1038/23301

Zusammenfassung

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.

Zusammenfassung in einer weiteren Sprache

Fachgebiet (DDC)
570 Biowissenschaften, Biologie

Schlagwörter

Konferenz

Rezension
undefined / . - undefined, undefined

Forschungsvorhaben

Organisationseinheiten

Zeitschriftenheft

Zugehörige Datensätze in KOPS

Zitieren

ISO 690DEUERLING, Elke, Agnes SCHULZE-SPECKING, Toshifumi TOMOYASU, Axel MOGK, Bernd BUKAU, 1999. Trigger factor and DnaK cooperate in folding of newly synthesized proteins. In: Nature. 1999, 400(6745), pp. 693-696. ISSN 0028-0836. Available under: doi: 10.1038/23301
BibTex
@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}
}
RDF
<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/123456789/8650">
    <dc:rights>Attribution-NonCommercial-NoDerivs 2.0 Generic</dc:rights>
    <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>
    <dspace:isPartOfCollection rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/28"/>
    <dc:language>eng</dc:language>
    <dc:contributor>Mogk, Axel</dc:contributor>
    <foaf:homepage rdf:resource="http://localhost:8080/"/>
    <dcterms:hasPart rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/8650/1/Trigger_factor_and_DnaK_cooperate_in_folding_of_newly_synthesized_proteins.pdf"/>
    <dc:format>application/pdf</dc:format>
    <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/8650"/>
    <dspace:hasBitstream rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/8650/1/Trigger_factor_and_DnaK_cooperate_in_folding_of_newly_synthesized_proteins.pdf"/>
    <void:sparqlEndpoint rdf:resource="http://localhost/fuseki/dspace/sparql"/>
    <dc:creator>Tomoyasu, Toshifumi</dc:creator>
    <dc:creator>Mogk, Axel</dc:creator>
    <dc:contributor>Schulze-Specking, Agnes</dc:contributor>
    <dcterms:rights rdf:resource="http://creativecommons.org/licenses/by-nc-nd/2.0/"/>
    <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>
    <dcterms:isPartOf rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/28"/>
    <dc:creator>Schulze-Specking, Agnes</dc:creator>
  </rdf:Description>
</rdf:RDF>

Interner Vermerk

xmlui.Submission.submit.DescribeStep.inputForms.label.kops_note_fromSubmitter

Kontakt
URL der Originalveröffentl.

Prüfdatum der URL

Prüfungsdatum der Dissertation

Finanzierungsart

Kommentar zur Publikation

Allianzlizenz
Corresponding Authors der Uni Konstanz vorhanden
Internationale Co-Autor:innen
Universitätsbibliographie
Nein
Begutachtet
Diese Publikation teilen