Publikation: Small heat shock proteins, ClpB and the DnaK system form a functional triade in reversing protein aggregation
Lade...
Dateien
Datum
2003
Autor:innen
Herausgeber:innen
ISSN der Zeitschrift
Electronic ISSN
ISBN
Bibliografische Daten
Verlag
Schriftenreihe
Auflagebezeichnung
URI (zitierfähiger Link)
DOI (zitierfähiger Link)
Internationale Patentnummer
Link zur Lizenz
Angaben zur Forschungsförderung
Projekt
Open Access-Veröffentlichung
Open Access Green
Sammlungen
Core Facility der Universität Konstanz
Titel in einer weiteren Sprache
Publikationstyp
Zeitschriftenartikel
Publikationsstatus
Published
Erschienen in
Molecular Microbiology. 2003, 50(2), pp. 585-595. eISSN 1365-2958. Available under: doi: 10.1046/j.1365-2958.2003.03710.x
Zusammenfassung
Small heat shock proteins (sHsps) can efficiently prevent the aggregation of unfolded proteins in vitro. However, how this in vitro activity translates to function in vivo is poorly understood. We demonstrate that sHsps of Escherichia coli, IbpA and IbpB, co-operate with ClpB and the DnaK system in vitro and in vivo, forming a functional triade of chaperones. IbpA/IbpB and ClpB support independently and co-operatively the DnaK system in reversing protein aggregation. A ΔibpAB ΔclpB double mutant exhibits strongly increased protein aggregation at 42ºC compared with the single mutants. sHsp and ClpB function become essential for cell viability at 37ºC if DnaK levels are reduced. The DnaK requirement for growth is increasingly higher for ΔibpAB, ΔclpB, and the double ΔibpAB ΔclpB mutant cells, establishing the positions of sHsps and ClpB in this chaperone triade.
Zusammenfassung in einer weiteren Sprache
Fachgebiet (DDC)
570 Biowissenschaften, Biologie
Schlagwörter
Konferenz
Rezension
undefined / . - undefined, undefined
Zitieren
ISO 690
MOGK, Axel, Elke DEUERLING, Sonja VORDERWÜLBECKE, Elizabeth VIERLING, Bernd BUKAU, 2003. Small heat shock proteins, ClpB and the DnaK system form a functional triade in reversing protein aggregation. In: Molecular Microbiology. 2003, 50(2), pp. 585-595. eISSN 1365-2958. Available under: doi: 10.1046/j.1365-2958.2003.03710.xBibTex
@article{Mogk2003Small-6978,
year={2003},
doi={10.1046/j.1365-2958.2003.03710.x},
title={Small heat shock proteins, ClpB and the DnaK system form a functional triade in reversing protein aggregation},
number={2},
volume={50},
journal={Molecular Microbiology},
pages={585--595},
author={Mogk, Axel and Deuerling, Elke and Vorderwülbecke, Sonja and Vierling, Elizabeth 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/123456789/6978">
<dcterms:title>Small heat shock proteins, ClpB and the DnaK system form a functional triade in reversing protein aggregation</dcterms:title>
<dc:creator>Bukau, Bernd</dc:creator>
<dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:30:35Z</dc:date>
<dc:contributor>Vierling, Elizabeth</dc:contributor>
<dc:creator>Vierling, Elizabeth</dc:creator>
<dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:30:35Z</dcterms:available>
<dc:creator>Deuerling, Elke</dc:creator>
<dc:creator>Vorderwülbecke, Sonja</dc:creator>
<dc:contributor>Mogk, Axel</dc:contributor>
<dc:rights>Attribution-NonCommercial-NoDerivs 2.0 Generic</dc:rights>
<dc:contributor>Bukau, Bernd</dc:contributor>
<dcterms:bibliographicCitation>First publ. in: Molecular Microbiology 50 (2003), 2, pp. 585-595</dcterms:bibliographicCitation>
<dc:language>eng</dc:language>
<dspace:isPartOfCollection rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/28"/>
<dcterms:isPartOf rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/28"/>
<dc:creator>Mogk, Axel</dc:creator>
<foaf:homepage rdf:resource="http://localhost:8080/"/>
<dcterms:issued>2003</dcterms:issued>
<dc:contributor>Deuerling, Elke</dc:contributor>
<dspace:hasBitstream rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/6978/1/Small_heat_shock_proteins.pdf"/>
<dc:contributor>Vorderwülbecke, Sonja</dc:contributor>
<dc:format>application/pdf</dc:format>
<bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/6978"/>
<void:sparqlEndpoint rdf:resource="http://localhost/fuseki/dspace/sparql"/>
<dcterms:rights rdf:resource="http://creativecommons.org/licenses/by-nc-nd/2.0/"/>
<dcterms:abstract xml:lang="eng">Small heat shock proteins (sHsps) can efficiently prevent the aggregation of unfolded proteins in vitro. However, how this in vitro activity translates to function in vivo is poorly understood. We demonstrate that sHsps of Escherichia coli, IbpA and IbpB, co-operate with ClpB and the DnaK system in vitro and in vivo, forming a functional triade of chaperones. IbpA/IbpB and ClpB support independently and co-operatively the DnaK system in reversing protein aggregation. A ΔibpAB ΔclpB double mutant exhibits strongly increased protein aggregation at 42ºC compared with the single mutants. sHsp and ClpB function become essential for cell viability at 37ºC if DnaK levels are reduced. The DnaK requirement for growth is increasingly higher for ΔibpAB, ΔclpB, and the double ΔibpAB ΔclpB mutant cells, establishing the positions of sHsps and ClpB in this chaperone triade.</dcterms:abstract>
<dcterms:hasPart rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/6978/1/Small_heat_shock_proteins.pdf"/>
</rdf:Description>
</rdf:RDF>Interner Vermerk
xmlui.Submission.submit.DescribeStep.inputForms.label.kops_note_fromSubmitter
Prüfungsdatum der Dissertation
Finanzierungsart
Kommentar zur Publikation
Allianzlizenz
Corresponding Authors der Uni Konstanz vorhanden
Internationale Co-Autor:innen
Universitätsbibliographie
Nein
