TY - JOUR
T1 - Analysis of the elements of catabolite repression in Clostridium acetobutylicum ATCC 824
AU - Tangney, Martin
AU - Galinier, Anne
AU - Deutscher, Josef
AU - Mitchell, Wilfrid J.
PY - 2003
Y1 - 2003
N2 - 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. subtilisand 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. Copyright © 2003 S. Karger AG, Basel.
AB - 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. subtilisand 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. Copyright © 2003 S. Karger AG, Basel.
KW - CcpA
KW - HPr
KW - Phosphotransferase system
KW - Protein kinase
UR - http://www.scopus.com/inward/record.url?scp=0344197722&partnerID=8YFLogxK
U2 - 10.1159/000073403
DO - 10.1159/000073403
M3 - Article
C2 - 14593248
SN - 1660-2412
VL - 6
SP - 6
EP - 11
JO - Journal of Molecular Microbiology and Biotechnology
JF - Journal of Molecular Microbiology and Biotechnology
IS - 1
ER -