Tangney, Martin, Deutscher, J, Galinier, A and Mitchell, Wilfred J (2003) Analysis of the elements of catabolite repression in Clostridium acetobutylicum. Journal of Molecular Microbiology and Biotechnology, 6 (1). pp. 6-11. ISSN 16602412
Full text not available from this repository. (Request a copy)Abstract/Description
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.
| Item Type: | Article |
|---|---|
| Print ISSN: | 16602412 |
| Uncontrolled Keywords: | Phosphotransferase system; HPr; Protein kinase; CcpA; |
| University Divisions/Research Centres: | Faculty of Health, Life & Social Sciences |
| Dewey Decimal Subjects: | 600 Technology > 660 Chemical engineering 500 Science > 570 Life sciences; biology > 576 Genetics & evolution |
| Library of Congress Subjects: | T Technology > TP Chemical technology Q Science > QH Natural history > QH426 Genetics |
| Item ID: | 1681 |
| Depositing User: | RAE Import |
| Date Deposited: | 04 Jul 2008 11:35 |
| Last Modified: | 26 Aug 2011 14:58 |
| URI: | http://researchrepository.napier.ac.uk/id/eprint/1681 |
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