A proteomic study of corynebacterium glutamicum AAA+ protease FtsH

Lüdke, Alja; Krämer, Reinhard; Burkovski, Andreas; Schluesener, Daniela; Poetsch, Ansgar

A proteomic study of corynebacterium glutamicum AAA+ protease FtsH

Dateien

Lüdke_proteomic.pdfGröße: 2.54 MBDownloads: 306

Datum

2007

Autor:innen

Lüdke, Alja

Krämer, Reinhard

Burkovski, Andreas

Schluesener, Daniela

Poetsch, Ansgar

Open Access-Veröffentlichung

Open Access Green

Sammlungen

Biologie

Publikationstyp

Zeitschriftenartikel

Publikationsstatus

Published

Erschienen in

BMC Microbiology. 2007, 7(6), 10. ISSN 1471-2180. eISSN 1471-2180. Available under: doi: 10.1186/1471-2180-7-6

Zusammenfassung

Background: The influence of the membrane-bound AAA+ protease FtsH on membrane and cytoplasmic proteins of Corynebacterium glutamicum was investigated in this study. For the analysis of the membrane fraction, anion exchange chromatography was combined with SDS-PAGE, while the cytoplasmic protein fraction was studied by conventional two-dimensional gel electrophoresis.
Results: In contrast to the situation in other bacteria, deletion of C. glutamicum ftsH has no significant effect on growth in standard minimal medium or response to heat or osmotic stress. On the proteome level, deletion of the ftsH gene resulted in a strong increase of ten cytoplasmic and membrane proteins, namely biotin carboxylase/biotin carboxyl carrier protein (accBC), glyceraldehyde-3-phosphate dehydrogenase (gap), homocysteine methyltransferase (metE), malate synthase (aceB), isocitrate lyase (aceA), a conserved hypothetical protein (NCgl1985), succinate dehydrogenase A (sdhA), succinate dehydrogenase B (sdhB), succinate dehydrogenase CD (sdhCD), and glutamate binding protein (gluB), while 38 cytoplasmic and membrane-associated proteins showed a decreased abundance. The decreasing amount of succinate dehydrogenase A (sdhA) in the cytoplasmic fraction of the ftsH mutant compared to the wild type and its increasing abundance in the membrane fraction indicates that FtsH might be involved in the cleavage of a membrane anchor of this membrane-associated protein and by this changes its localization.
Conclusion: The data obtained hint to an involvement of C. glutamicum FtsH protease mainly in regulation of energy and carbon metabolism, while the protease is not involved in stress response,
as found in other bacteria.

Fachgebiet (DDC)

570 Biowissenschaften, Biologie

Zitieren

ISO 690

LÜDKE, Alja, Reinhard KRÄMER, Andreas BURKOVSKI, Daniela SCHLUESENER, Ansgar POETSCH, 2007. A proteomic study of corynebacterium glutamicum AAA+ protease FtsH. In: BMC Microbiology. 2007, 7(6), 10. ISSN 1471-2180. eISSN 1471-2180. Available under: doi: 10.1186/1471-2180-7-6

BibTex

@article{Ludke2007prote-16992,
  year={2007},
  doi={10.1186/1471-2180-7-6},
  title={A proteomic study of corynebacterium glutamicum AAA+ protease FtsH},
  number={6},
  volume={7},
  issn={1471-2180},
  journal={BMC Microbiology},
  author={Lüdke, Alja and Krämer, Reinhard and Burkovski, Andreas and Schluesener, Daniela and Poetsch, Ansgar},
  note={Article Number: 10}
}

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    <dcterms:abstract xml:lang="eng">Background: The influence of the membrane-bound AAA+ protease FtsH on membrane and cytoplasmic proteins of Corynebacterium glutamicum was investigated in this study. For the analysis of the membrane fraction, anion exchange chromatography was combined with SDS-PAGE, while the cytoplasmic protein fraction was studied by conventional two-dimensional gel electrophoresis.&lt;br /&gt;Results: In contrast to the situation in other bacteria, deletion of C. glutamicum ftsH has no significant effect on growth in standard minimal medium or response to heat or osmotic stress. On the proteome level, deletion of the ftsH gene resulted in a strong increase of ten cytoplasmic and membrane proteins, namely biotin carboxylase/biotin carboxyl carrier protein (accBC), glyceraldehyde-3-phosphate dehydrogenase (gap), homocysteine methyltransferase (metE), malate synthase (aceB), isocitrate lyase (aceA), a conserved hypothetical protein (NCgl1985), succinate dehydrogenase A (sdhA), succinate dehydrogenase B (sdhB), succinate dehydrogenase CD (sdhCD), and glutamate binding protein (gluB), while 38 cytoplasmic and membrane-associated proteins showed a decreased abundance. The decreasing amount of succinate dehydrogenase A (sdhA) in the cytoplasmic fraction of the ftsH mutant compared to the wild type and its increasing abundance in the membrane fraction indicates that FtsH might be involved in the cleavage of a membrane anchor of this membrane-associated protein and by this changes its localization.&lt;br /&gt;Conclusion: The data obtained hint to an involvement of C. glutamicum FtsH protease mainly in regulation of energy and carbon metabolism, while the protease is not involved in stress response,&lt;br /&gt;as found in other bacteria.</dcterms:abstract>
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