@article{Strosser2004-10Regul-17283,
  year={2004},
  doi={10.1111/j.1365-2958.2004.04247.x},
  title={Regulation of GlnK activity : modification, membrane sequestration and proteolysis as regulatory principles in the network of nitrogen control in Corynebacterium glutamicum},
  number={1},
  volume={54},
  issn={0950-382X},
  journal={Molecular Microbiology},
  pages={132--147},
  author={Strösser, Julia and Lüdke, Alja and Schaffer, Steffen and Krämer, Reinhard and Burkovski, Andreas}
}

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    <dc:creator>Burkovski, Andreas</dc:creator>
    <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2012-01-31T09:45:05Z</dcterms:available>
    <dc:contributor>Lüdke, Alja</dc:contributor>
    <dc:contributor>Strösser, Julia</dc:contributor>
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    <dc:creator>Krämer, Reinhard</dc:creator>
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    <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2012-01-31T09:45:05Z</dc:date>
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    <dc:creator>Lüdke, Alja</dc:creator>
    <dcterms:abstract xml:lang="eng">PII-type signal transduction proteins play a central role in nitrogen regulation in many bacteria. In response to the intracellular nitrogen status, these proteins are rendered in their function and interaction with other proteins by modification/demodification events, e.g. by phosphorylation or uridylylation. In this study, we show that GlnK, the only PII-type protein in Corynebacterium glutamicum, is adenylylated in response to nitrogen starvation and deadenylylated when the nitrogen supply improves again. Both processes depend on the GlnD protein. As shown by mutant analyses, the modifying activity of this enzyme is located in the N-terminal part of the enzyme, while demodification depends on its C-terminal domain. Besides its modification status, the GlnK protein changes its intracellular localization in response to changes of the cellular nitrogen supply. While it is present in the cytoplasm during nitrogen starvation, the GlnK protein is sequestered to the cytoplasmic membrane in response to an ammonium pulse following a nitrogen starvation period. About 2–5% of the GlnK pool is located at the cytoplasmic membrane after ammonium addition. GlnK binding to the cytoplasmic membrane depends on the ammonium transporter AmtB, which is encoded in the same transcriptional unit as GlnK and GlnD, the amtB-glnKglnD operon. In contrast, the structurally related methylammonium/ammonium permease AmtA does not bind GlnK. The membrane-bound GlnK protein is stable, most likely to inactivate AmtB-dependent ammonium transport in order to prevent a detrimental futile cycle under post-starvation ammonium-rich conditions, while the majority of GlnK is degraded within 2–4 min. Proteolysis in the transition period from nitrogen starvation to nitrogen-rich growth seems to be specific for GlnK; other proteins of the nitrogen metabolism, such as glutamine synthetase, or proteins unrelated to ammonium assimilation, such as enolase and ATP synthase subunit F1b, are stable under these conditions. Our analyses of different mutant strains have shown that at least three different proteases influence the degradation of GlnK, namely FtsH, the ClpCP and the ClpXP protease&lt;br /&gt;complex.</dcterms:abstract>
    <dc:contributor>Krämer, Reinhard</dc:contributor>
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    <dc:contributor>Schaffer, Steffen</dc:contributor>
    <dcterms:bibliographicCitation>First publ. in: Molecular Microbiology ; 54 (2004), 1. - pp. 132-147</dcterms:bibliographicCitation>
    <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/17283"/>
    <dcterms:title>Regulation of GlnK activity : modification, membrane sequestration and proteolysis as regulatory principles in the network of nitrogen control in Corynebacterium glutamicum</dcterms:title>
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    <dc:creator>Schaffer, Steffen</dc:creator>
    <dc:contributor>Burkovski, Andreas</dc:contributor>
    <dc:creator>Strösser, Julia</dc:creator>
    <dcterms:issued>2004-10</dcterms:issued>
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