@article{Schneider2013-06-15Impro-23461,
  year={2013},
  doi={10.1016/j.bmc.2013.03.063},
  title={Improving bioorthogonal protein ubiquitylation by click reaction},
  number={12},
  volume={21},
  issn={0968-0896},
  journal={Bioorganic & Medicinal Chemistry},
  pages={3430--3435},
  author={Schneider, Daniel and Schneider, Tatjana and Rösner, Daniel and Scheffner, Martin and Marx, Andreas}
}

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    <dcterms:title>Improving bioorthogonal protein ubiquitylation by click reaction</dcterms:title>
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    <dc:contributor>Scheffner, Martin</dc:contributor>
    <dc:contributor>Rösner, Daniel</dc:contributor>
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    <dc:language>eng</dc:language>
    <dc:contributor>Schneider, Daniel</dc:contributor>
    <dcterms:bibliographicCitation>Bioorganic &amp; Medicinal Chemistry ; 21 (2013), 12. - S. 3430-3435</dcterms:bibliographicCitation>
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    <dc:creator>Schneider, Tatjana</dc:creator>
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    <dcterms:abstract xml:lang="eng">Posttranslational modification of proteins with ubiquitin (ubiquitylation) regulates numerous cellular processes. Besides functioning as a signal for proteasomal degradation, ubiquitylation has also non-proteolytic functions by altering the biochemical properties of the modified protein. To investigate the effect(s) of ubiquitylation on the properties of a protein, sufficient amounts of homogenously and well-defined ubiquitylated proteins are required. Here, we report on the elaboration of a method for the generation of high amounts of site-specifically mono-ubiquitylated proteins. Firstly, a one-step affinity purification scheme was developed for ubiquitin containing the unnatural amino acid azidohomoalanine at the C-terminal position. This ubiquitin was conjugated in a click reaction to recombinant DNA polymerase beta, equipped with an alkyne function at a distinct position. Secondly, addition of defined amounts of SDS to the reaction significantly improved product formation. With these two technical improvements, we have developed a straight forward procedure for the efficient generation of site-specifically ubiquitylated proteins that can be used to study the effect(s) of ubiquitylation on the activities/ properties of a protein.</dcterms:abstract>
    <dcterms:issued>2013-06-15</dcterms:issued>
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    <dc:creator>Schneider, Daniel</dc:creator>
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    <dc:contributor>Marx, Andreas</dc:contributor>
    <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2013-06-21T09:14:51Z</dc:date>
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    <dc:creator>Rösner, Daniel</dc:creator>
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