Publikation:

Trigger factor peptidyl-prolyl cis/trans isomerase activity is not essential for the folding of cytosolic proteins in Escherichia coli

Lade...
Vorschaubild

Datum

2004

Autor:innen

Kramer, Günter
Patzelt, Holger
Rauch, Thomas
Kurz, Thorben A.
Vorderwülbecke, Sonja
Bukau, Bernd

Herausgeber:innen

Kontakt

ISSN der Zeitschrift

Electronic ISSN

ISBN

Bibliografische Daten

Verlag

Schriftenreihe

Auflagebezeichnung

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

Journal of Biological Chemistry. 2004, 279(14), pp. 14165-14170. ISSN 0021-9258. eISSN 1083-351X. Available under: doi: 10.1074/jbc.M313635200

Zusammenfassung

The ribosome-associated Trigger Factor (TF) cooperates with the DnaK system to assist the folding of newly synthesized polypeptides in Escherichia coli. TF unifies two functions in one to promote proper protein folding in vitro. First, as a chaperone it binds to unfolded protein substrates, thereby preventing aggregation and supporting productive folding. Second, TF catalyzes the cis/trans isomerization of peptidyl-prolyl bonds, which can be a rate-limiting step in protein folding. Here, we investigated whether the peptidyl-prolyl cis/trans isomerase (PPIase) function is essential for the folding activity of TF in vitro and in vivo by separating these two TF activities through site-directed mutagenesis of the PPIase catalytic center. Of the four different TF variants carrying point mutations in the PPIase domain, only the exchange of the conserved residue Phe- 198 to Ala (TF F198A) abolished the PPIase activity of TF toward both a tetrapeptide and the model protein substrate RNase T1 in vitro. In contrast, all other activities of TF F198A tested were comparable with wild type TF. TF F198A retained a similar binding specificity toward membrane-bound peptides, assisted the refolding of denatured D-glyceraldehyde-3-phosphate dehydrogenase in vitro, and associated with nascent polypeptides in an in vitro transcription/translation system. Importantly, expression of the TF F198A encoding gene complemented the synthetic lethality of ΔtigΔdnaK cells and prevented global protein misfolding at temperatures between 20 and 34°C in these cells. We conclude that the PPIase activity is not required for the function of TF in folding of newly synthesized proteins.

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 690KRAMER, Günter, Holger PATZELT, Thomas RAUCH, Thorben A. KURZ, Sonja VORDERWÜLBECKE, Bernd BUKAU, Elke DEUERLING, 2004. Trigger factor peptidyl-prolyl cis/trans isomerase activity is not essential for the folding of cytosolic proteins in Escherichia coli. In: Journal of Biological Chemistry. 2004, 279(14), pp. 14165-14170. ISSN 0021-9258. eISSN 1083-351X. Available under: doi: 10.1074/jbc.M313635200
BibTex
@article{Kramer2004Trigg-8542,
  year={2004},
  doi={10.1074/jbc.M313635200},
  title={Trigger factor peptidyl-prolyl cis/trans isomerase activity is not essential for the folding of cytosolic proteins in Escherichia coli},
  number={14},
  volume={279},
  issn={0021-9258},
  journal={Journal of Biological Chemistry},
  pages={14165--14170},
  author={Kramer, Günter and Patzelt, Holger and Rauch, Thomas and Kurz, Thorben A. and Vorderwülbecke, Sonja and Bukau, Bernd and Deuerling, Elke}
}
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/123456789/8542">
    <dc:contributor>Patzelt, Holger</dc:contributor>
    <dc:creator>Vorderwülbecke, Sonja</dc:creator>
    <dcterms:isPartOf rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/28"/>
    <dc:creator>Bukau, Bernd</dc:creator>
    <dspace:hasBitstream rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/8542/1/Trigger_Factor_Peptidyl_prolyl_cistrans_Isomerase_Activity.pdf"/>
    <dc:contributor>Deuerling, Elke</dc:contributor>
    <dc:creator>Kurz, Thorben A.</dc:creator>
    <dcterms:rights rdf:resource="http://creativecommons.org/licenses/by-nc-nd/2.0/"/>
    <dc:creator>Patzelt, Holger</dc:creator>
    <dc:contributor>Bukau, Bernd</dc:contributor>
    <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">2011-03-24T17:44:31Z</dc:date>
    <dc:contributor>Kurz, Thorben A.</dc:contributor>
    <dcterms:abstract xml:lang="eng">The ribosome-associated Trigger Factor (TF) cooperates with the DnaK system to assist the folding of newly synthesized polypeptides in Escherichia coli. TF unifies two functions in one to promote proper protein folding in vitro. First, as a chaperone it binds to unfolded protein substrates, thereby preventing aggregation and supporting productive folding. Second, TF catalyzes the cis/trans isomerization of peptidyl-prolyl bonds, which can be a rate-limiting step in protein folding. Here, we investigated whether the peptidyl-prolyl cis/trans isomerase (PPIase) function is essential for the folding activity of TF in vitro and in vivo by separating these two TF activities through site-directed mutagenesis of the PPIase catalytic center. Of the four different TF variants carrying point mutations in the PPIase domain, only the exchange of the conserved residue Phe- 198 to Ala (TF F198A) abolished the PPIase activity of TF toward both a tetrapeptide and the model protein substrate RNase T1 in vitro. In contrast, all other activities of TF F198A tested were comparable with wild type TF. TF F198A retained a similar binding specificity toward membrane-bound peptides, assisted the refolding of denatured D-glyceraldehyde-3-phosphate dehydrogenase in vitro, and associated with nascent polypeptides in an in vitro transcription/translation system. Importantly, expression of the TF F198A encoding gene complemented the synthetic lethality of ΔtigΔdnaK cells and prevented global protein misfolding at temperatures between 20 and 34°C in these cells. We conclude that the PPIase activity is not required for the function of TF in folding of newly synthesized proteins.</dcterms:abstract>
    <dc:contributor>Vorderwülbecke, Sonja</dc:contributor>
    <dcterms:title>Trigger factor peptidyl-prolyl cis/trans isomerase activity is not essential for the folding of cytosolic proteins in Escherichia coli</dcterms:title>
    <dc:format>application/pdf</dc:format>
    <dc:contributor>Kramer, Günter</dc:contributor>
    <dcterms:hasPart rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/8542/1/Trigger_Factor_Peptidyl_prolyl_cistrans_Isomerase_Activity.pdf"/>
    <dcterms:issued>2004</dcterms:issued>
    <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:44:31Z</dcterms:available>
    <void:sparqlEndpoint rdf:resource="http://localhost/fuseki/dspace/sparql"/>
    <dc:contributor>Rauch, Thomas</dc:contributor>
    <dc:creator>Kramer, Günter</dc:creator>
    <dc:creator>Rauch, Thomas</dc:creator>
    <dc:language>eng</dc:language>
    <dc:rights>Attribution-NonCommercial-NoDerivs 2.0 Generic</dc:rights>
    <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/8542"/>
    <dcterms:bibliographicCitation>First publ. in: Journal of Biological Chemistry 279 (2004), 14, pp. 14165 14170</dcterms:bibliographicCitation>
    <dc:creator>Deuerling, Elke</dc:creator>
    <foaf:homepage rdf:resource="http://localhost:8080/"/>
  </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