Open AccessInteraction of GapA with HPr and Its Homologue, Crh: Novel Levels of Regulation of a Key Step of Glycolysis in Bacillus subtilis ?
Author(s) -
Frédérique Pompeo,
Jennifer Luciano,
Anne Galinier
Publication year - 2007
Publication title -
journal of bacteriology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.652
H-Index - 246
eISSN - 1067-8832
pISSN - 0021-9193
DOI - 10.1128/jb.01575-06
Subject(s) - bacillus subtilis , biology , glyceraldehyde 3 phosphate dehydrogenase , glycolysis , dehydrogenase , biochemistry , glyceraldehyde , enzyme , phosphorylation , bacteria , genetics
InBacillus subtilis cells, we identified a new partner of HPr, an enzyme of the glycolysis pathway, the glyceraldehyde-3-phosphate dehydrogenase GapA. We showed that, in vitro, phosphorylated and unphosphorylated forms of HPr and its homologue, Crh, could interact with GapA, but only their seryl-phosphorylated forms were able to inhibit its activity.