KOPS - The Institutional Repository of the University of Konstanz

The ubiquitin-protein ligase activity of Hdm2 is inhibited by nucleic acids

Aufgrund von Vorbereitungen auf eine neue Version von KOPS, können kommenden Montag und Dienstag keine Publikationen eingereicht werden. (Due to preparations for a new version of KOPS, no publications can be submitted next Monday and Tuesday.)

The ubiquitin-protein ligase activity of Hdm2 is inhibited by nucleic acids

Cite This

Files in this item

Files Size Format View

There are no files associated with this item.

LINARES, Laëtitia K., Martin SCHEFFNER, 2003. The ubiquitin-protein ligase activity of Hdm2 is inhibited by nucleic acids. In: FEBS Letters. 554(1-2), pp. 73-76. ISSN 0014-5793. eISSN 0014-5793. Available under: doi: 10.1016/S0014-5793(03)01108-6

@article{Linares2003ubiqu-42781, title={The ubiquitin-protein ligase activity of Hdm2 is inhibited by nucleic acids}, year={2003}, doi={10.1016/S0014-5793(03)01108-6}, number={1-2}, volume={554}, issn={0014-5793}, journal={FEBS Letters}, pages={73--76}, author={Linares, Laëtitia K. and Scheffner, Martin} }

<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/rdf/resource/123456789/42781"> <dcterms:isPartOf rdf:resource="https://kops.uni-konstanz.de/rdf/resource/123456789/28"/> <dspace:isPartOfCollection rdf:resource="https://kops.uni-konstanz.de/rdf/resource/123456789/28"/> <dc:language>eng</dc:language> <void:sparqlEndpoint rdf:resource="http://localhost/fuseki/dspace/sparql"/> <dcterms:abstract xml:lang="eng">The proto‐oncoprotein Hdm2 is a member of the RING finger‐type family of ubiquitin–protein ligases E3. The RING finger domain is assumed to mediate the specific interaction of an E3 with its cognate ubiquitin‐conjugating enzyme E2, which catalyzes the covalent attachment of ubiquitin to substrate proteins. In addition, the RING finger domain of Hdm2 is involved in Hdm2 homooligomer formation and has the capacity to bind to RNA in a sequence‐specific manner. Here we report that interaction with nucleic acids interferes with both Hdm2/Hdm2 complex formation and auto‐ubiquitination of Hdm2 in vitro. Furthermore, although binding of Hdm2 to the tumor suppressor p53 is not inhibited by nucleic acids, Hdm2‐mediated ubiquitination of p53 is significantly decreased. Taken together, these results provide the first example of an E3 whose activity can be regulated by direct interaction with nucleic acids.</dcterms:abstract> <dcterms:title>The ubiquitin-protein ligase activity of Hdm2 is inhibited by nucleic acids</dcterms:title> <foaf:homepage rdf:resource="http://localhost:8080/jspui"/> <dc:creator>Linares, Laëtitia K.</dc:creator> <dc:contributor>Scheffner, Martin</dc:contributor> <dc:contributor>Linares, Laëtitia K.</dc:contributor> <dcterms:issued>2003</dcterms:issued> <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2018-07-04T16:43:05Z</dcterms:available> <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2018-07-04T16:43:05Z</dc:date> <dc:creator>Scheffner, Martin</dc:creator> <bibo:uri rdf:resource="https://kops.uni-konstanz.de/handle/123456789/42781"/> </rdf:Description> </rdf:RDF>

This item appears in the following Collection(s)

Search KOPS


Browse

My Account