Marie-Claude Kilhoffer

TL;DR: The results suggest that CCR of certain catabolic operons requires, in addition to CcpA, ATP-dependent phosphorylation of Crh, and HPr at Ser-46, as well as the discovery of a new B. subtilis gene encoding a HPr-like protein, Crh (for catabolite repression HPr).

TL;DR: In this paper, the Bacillus subtilis hprK and hprP genes were cloned and the encoded HPr kinase and P-Ser-HPr phosphatase formed a new family of protein kinases.

TL;DR: Cl cloning of the Bacillus subtilis hprK and hprP genes and characterization of the encoded HPr kinase and P-Ser-HPr phosphatase reveal that the HPr modifying/demodifying enzymes were thought to exist only in Gram-positive bacteria, but a sequence comparison revealed that they also are present in several Gram-negative pathogenic bacteria.

TL;DR: The results provide strong evidence for a regulatory role for Ca2+ in bacterial cells in Bacillus subtilis, a Gram-positive bacterium, and four putativeCa2+ binding proteins were found, including AhpC, which appears to be regulated by Ca2+.

TL;DR: The altered calcium binding activity of calmodulins (CaM) with point mutations can be restored toward that of wild type CaMs by the formation of a complex between CaM and a CaM binding sequence, and the possibility that the selective functional effects of in vivo mutations in the calcium binding sites of CaM might be partially due to the ability to select and utilize CaM conformations with calcium ligation structures different from the so-called canonical EF-hand is raised.