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Analysis of the elements of catabolite repression in Clostridium acetobutylicum.

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 1464-1801

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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: 1464-1801
Electronic ISSN: 1660 2412
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: 07 Jun 2013 14:31
URI: http://researchrepository.napier.ac.uk/id/eprint/1681

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