A cradle for new proteins : trigger factor at the ribosome

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MAIER, Timm, Lars FERBITZ, Elke DEUERLING, Nenad BAN, 2005. A cradle for new proteins : trigger factor at the ribosome. In: Current Opinion in Structural Biology. 15(2), pp. 204-212. ISSN 0959-440X

@article{Maier2005cradl-7052, title={A cradle for new proteins : trigger factor at the ribosome}, year={2005}, doi={10.1016/j.sbi.2005.03.005}, number={2}, volume={15}, issn={0959-440X}, journal={Current Opinion in Structural Biology}, pages={204--212}, author={Maier, Timm and Ferbitz, Lars and Deuerling, Elke and Ban, Nenad} }

<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/123456789/7052"> <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:31:08Z</dc:date> <dcterms:title>A cradle for new proteins : trigger factor at the ribosome</dcterms:title> <dc:creator>Ban, Nenad</dc:creator> <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/7052"/> <dc:contributor>Maier, Timm</dc:contributor> <dcterms:abstract xml:lang="eng">Newly synthesized proteins leave the ribosome through a narrow tunnel in the large subunit. During ongoing synthesis, nascent protein chains are particularly sensitive to aggregation and degradation because they emerge from the ribosome in an unfolded state. In bacteria, the first protein to interact with nascent chains and facilitate their folding is the ribosomeassociated chaperone trigger factor. Recently, crystal structures of trigger factor and of its ribosome-binding domain in complex with the large ribosomal subunit revealed that the chaperone adopts an extended dragon-shaped fold with a large hydrophobic cradle, which arches over the exit of the ribosomal tunnel and shields newly synthesized proteins. These structural results, together with recent biochemical data on trigger factor and its interplay with other chaperones and factors that interact with the nascent chain, provide a comprehensive view of the role of trigger factor during cotranslational protein folding.</dcterms:abstract> <dc:creator>Ferbitz, Lars</dc:creator> <dc:contributor>Ferbitz, Lars</dc:contributor> <dc:rights>deposit-license</dc:rights> <dcterms:rights rdf:resource="https://creativecommons.org/licenses/by-nc-nd/2.0/legalcode"/> <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:31:08Z</dcterms:available> <dc:creator>Maier, Timm</dc:creator> <dc:contributor>Ban, Nenad</dc:contributor> <dcterms:issued>2005</dcterms:issued> <dc:language>eng</dc:language> <dc:contributor>Deuerling, Elke</dc:contributor> <dc:format>application/pdf</dc:format> <dc:creator>Deuerling, Elke</dc:creator> <dcterms:bibliographicCitation>First publ. in: Current Opinion in Structural Biology 15 (2005), 2, pp. 204 212</dcterms:bibliographicCitation> </rdf:Description> </rdf:RDF>

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