Prof Martin Tangney M.Tangney@napier.ac.uk
Professor
Analysis of the elements of catabolite repression in Clostridium acetobutylicum.
Tangney, Martin; Deutscher, J; Galinier, A; Mitchell, Wilfred J
Authors
J Deutscher
A Galinier
Wilfred J Mitchell
Abstract
The ptsH gene, encoding the phosphotransferase protein HPr, from Clostridium acetobutylicum ATCC 824 was identified from the genome sequence, cloned and shown to complement a ptsH mutant of Escherichia coli. The deduced protein sequence shares significant homology with HPr proteins from other low-GC gram-positive bacteria, although the highly conserved sequence surrounding the Ser-46 phosphorylation site is not well preserved in the clostridial protein. Nevertheless, the HPr was phosphorylated in an ATP-dependent manner in cell-free extracts of C. acetobutylicum. Furthermore, purified His-tagged HPr from Bacillus subtilis was also a substrate for the clostridial HPr kinase/phosphorylase. This phosphorylation reaction is a key step in the mechanism of carbon catabolite repression proposed to operate in B. subtilis and other low-GC gram-positive bacteria. Putative genes encoding the HPr kinase/phosphorylase and the other element of this model, namely the catabolite control protein CcpA, were identified from the C. acetobutylicum genome sequence, suggesting that a similar mechanism of carbon catabolite repression may operate in this industrially important organism.
Citation
Tangney, M., Deutscher, J., Galinier, A., & Mitchell, W. J. (2003). Analysis of the elements of catabolite repression in Clostridium acetobutylicum. Journal of Molecular Microbiology and Biotechnology, 6, 6-11. https://doi.org/10.1159/000073403
Journal Article Type | Article |
---|---|
Publication Date | Oct 1, 2003 |
Deposit Date | Jul 4, 2008 |
Print ISSN | 1464-1801 |
Electronic ISSN | 1660-2412 |
Publisher | Karger Publishers |
Peer Reviewed | Peer Reviewed |
Volume | 6 |
Pages | 6-11 |
DOI | https://doi.org/10.1159/000073403 |
Keywords | Phosphotransferase system; HPr; Protein kinase; CcpA; |
Public URL | http://researchrepository.napier.ac.uk/id/eprint/1681 |
Publisher URL | http://dx.doi.org/10.1159/000073403 |
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