Three-state equilibrium of Escherichia coli trigger factor

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PATZELT, Holger, Günter KRAMER, Thomas RAUCH, Hans-Joachim SCHÖNFELD, Bernd BUKAU, Elke DEUERLING, 2002. Three-state equilibrium of Escherichia coli trigger factor. In: Biological Chemistry. 383(10), pp. 1611-1619. ISSN 1431-6730

@article{Patzelt2002Three-7977, title={Three-state equilibrium of Escherichia coli trigger factor}, year={2002}, doi={ 10.1515/BC.2002.182}, number={10}, volume={383}, issn={1431-6730}, journal={Biological Chemistry}, pages={1611--1619}, author={Patzelt, Holger and Kramer, Günter and Rauch, Thomas and Schönfeld, Hans-Joachim and Bukau, Bernd and Deuerling, Elke} }

<rdf:RDF xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" xmlns:bibo="http://purl.org/ontology/bibo/" xmlns:dc="http://purl.org/dc/elements/1.1/" xmlns:dcterms="http://purl.org/dc/terms/" xmlns:xsd="http://www.w3.org/2001/XMLSchema#" > <rdf:Description rdf:about="https://kops.uni-konstanz.de/rdf/resource/123456789/7977"> <dc:creator>Bukau, Bernd</dc:creator> <dc:creator>Schönfeld, Hans-Joachim</dc:creator> <dcterms:bibliographicCitation>First publ. in: Biological Chemistry, 383 (2002), pp. 1611-1619</dcterms:bibliographicCitation> <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:39:00Z</dcterms:available> <dcterms:issued>2002</dcterms:issued> <dcterms:title>Three-state equilibrium of Escherichia coli trigger factor</dcterms:title> <dcterms:rights rdf:resource="https://creativecommons.org/licenses/by-nc-nd/2.0/legalcode"/> <dc:contributor>Rauch, Thomas</dc:contributor> <dc:contributor>Schönfeld, Hans-Joachim</dc:contributor> <dcterms:abstract xml:lang="eng">Trigger Factor (TF) is the first chaperone that interacts with nascent chains of cytosolic proteins in Escherichia coli. Although its chaperone activity requires association with ribosomes, TF is present in vivo in a 2 3 fold molar excess over ribosomes and a fraction of it is not ribosome-associated after cell lysis. Here we show that TF follows a three-state equilibrium. Size exclusion chromatography, crosslinking and analytical ultracentrifugation revealed that uncomplexed TF dimerizes with an apparent Kd of 18 μM. Dimerization is mediated by the N-terminal ribosome binding domain and the C-terminal domain of TF, whereas the central peptidyl prolyl isomerase (PPIase) and substrate binding domain does not contribute to dimerization. Crosslinking experiments showed that TF is monomeric in its ribosome-associated state. Quantitative analysis of TF binding to ribosomes revealed a dissociation constant for the TF-ribosome complex of approximately 1.2 μM. From these data we estimate that in vivo most of the ribosomes are in complex with monomeric TF. Uncomplexed TF, however, is in a monomer-dimer equilibrium with approximately two thirds of TF existing in a dimeric state.</dcterms:abstract> <dc:format>application/pdf</dc:format> <dc:language>eng</dc:language> <dc:contributor>Bukau, Bernd</dc:contributor> <dc:creator>Patzelt, Holger</dc:creator> <dc:creator>Rauch, Thomas</dc:creator> <dc:contributor>Patzelt, Holger</dc:contributor> <dc:contributor>Kramer, Günter</dc:contributor> <dc:rights>deposit-license</dc:rights> <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/7977"/> <dc:creator>Deuerling, Elke</dc:creator> <dc:contributor>Deuerling, Elke</dc:contributor> <dc:creator>Kramer, Günter</dc:creator> <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:39:00Z</dc:date> </rdf:Description> </rdf:RDF>

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