A proteomic study of Corynebacterium glutamicum AAA+ protease FtsH

doi:10.1186/1471-2180-7-6

BMC Microbiology

Volume 7

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Lüdke A
Krämer R
Burkovski A
Schluesener D
Poetsch A

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Krämer R
Burkovski A
Schluesener D
Poetsch A
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Research article

A proteomic study of Corynebacterium glutamicum AAA+ protease FtsH

Alja Lüdke¹ , Reinhard Krämer¹ , Andreas Burkovski¹^,2 , Daniela Schluesener³ and Ansgar Poetsch³

¹Institut für Biochemie, Universität zu Köln, Zülpicher Str. 47, 50674 Köln, Germany

²Lehrstuhl für Mikrobiologie, Friedrich-Alexander-Universität Erlangen-Nürnberg, Staudtstr. 5, 91058 Erlangen, Germany

³Lehrstuhl für Biochemie der Pflanzen, Ruhr-Universität Bochum, Universitätsstr. 150, 44801 Bochum, Germany

author email corresponding author email

BMC Microbiology 2007, 7:6doi:10.1186/1471-2180-7-6


Published:	25 January 2007

Abstract

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.