@article{Kienle2022-09-16Elect-58677,
  year={2022},
  doi={10.1038/s41467-022-33087-1},
  title={Electrostatic and steric effects underlie acetylation-induced changes in ubiquitin structure and function},
  number={1},
  volume={13},
  journal={Nature Communications},
  author={Kienle, Simon Maria and Schneider, Tobias and Stuber, Katrin and Globisch, Christoph and Jansen, Jasmin and Stengel, Florian and Peter, Christine and Marx, Andreas and Kovermann, Michael and Scheffner, Martin},
  note={This work was supported by the DFG (SFB969, Projects B3 and B9). C.P. and C.G. acknowledge support by the state of Baden-Württemberg (bwHPC) and by the DFG (INST 35/1134-1 FUGG); F.S. is grateful for funding by the DFG Emmy Noether Programme and the DFG Heisenberg Programme (STE 2517/1, STE 2517/5-1). Article Number: 5435}
}

<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/123456789/58677">
    <bibo:uri rdf:resource="https://kops.uni-konstanz.de/handle/123456789/58677"/>
    <dc:creator>Schneider, Tobias</dc:creator>
    <dspace:isPartOfCollection rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/28"/>
    <dc:contributor>Jansen, Jasmin</dc:contributor>
    <dspace:isPartOfCollection rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/29"/>
    <dc:creator>Stuber, Katrin</dc:creator>
    <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2022-09-22T11:06:49Z</dc:date>
    <dcterms:isPartOf rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/28"/>
    <dc:contributor>Marx, Andreas</dc:contributor>
    <dc:contributor>Stengel, Florian</dc:contributor>
    <dc:creator>Peter, Christine</dc:creator>
    <dc:contributor>Scheffner, Martin</dc:contributor>
    <dc:contributor>Stuber, Katrin</dc:contributor>
    <dc:creator>Globisch, Christoph</dc:creator>
    <dc:rights>Attribution 4.0 International</dc:rights>
    <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2022-09-22T11:06:49Z</dcterms:available>
    <dc:contributor>Kovermann, Michael</dc:contributor>
    <dcterms:issued>2022-09-16</dcterms:issued>
    <dspace:hasBitstream rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/58677/1/Kienle_2-5nlwjgr596492.pdf"/>
    <dc:contributor>Kienle, Simon Maria</dc:contributor>
    <dc:creator>Jansen, Jasmin</dc:creator>
    <dc:creator>Stengel, Florian</dc:creator>
    <foaf:homepage rdf:resource="http://localhost:8080/"/>
    <dc:language>eng</dc:language>
    <dc:contributor>Peter, Christine</dc:contributor>
    <dcterms:rights rdf:resource="http://creativecommons.org/licenses/by/4.0/"/>
    <dcterms:title>Electrostatic and steric effects underlie acetylation-induced changes in ubiquitin structure and function</dcterms:title>
    <dc:creator>Scheffner, Martin</dc:creator>
    <dcterms:abstract xml:lang="eng">Covalent attachment of ubiquitin (Ub) to proteins is a highly versatile posttranslational modification. Moreover, Ub is not only a modifier but itself is modified by phosphorylation and lysine acetylation. However, the functional consequences of Ub acetylation are poorly understood. By generation and comprehensive characterization of all seven possible mono-acetylated Ub variants, we show that each acetylation site has a particular impact on Ub structure. This is reflected in selective usage of the acetylated variants by different E3 ligases and overlapping but distinct interactomes, linking different acetylated variants to different cellular pathways. Notably, not only electrostatic but also steric effects contribute to acetylation-induced changes in Ub structure and, thus, function. Finally, we provide evidence that p300 acts as a position-specific Ub acetyltransferase and HDAC6 as a general Ub deacetylase. Our findings provide intimate insights into the structural and functional consequences of Ub acetylation and highlight the general importance of Ub acetylation.</dcterms:abstract>
    <void:sparqlEndpoint rdf:resource="http://localhost/fuseki/dspace/sparql"/>
    <dcterms:hasPart rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/58677/1/Kienle_2-5nlwjgr596492.pdf"/>
    <dc:contributor>Globisch, Christoph</dc:contributor>
    <dc:creator>Kovermann, Michael</dc:creator>
    <dc:creator>Kienle, Simon Maria</dc:creator>
    <dc:contributor>Schneider, Tobias</dc:contributor>
    <dc:creator>Marx, Andreas</dc:creator>
    <dcterms:isPartOf rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/29"/>
  </rdf:Description>
</rdf:RDF>