Open AccessDominant ptsH mutations of the gene coding for synthesis of the HPr protein of the phosphoenolpyruvate‐dependent phosphotransferase system in Escherichia coli K‐12 merodiploids
Author(s) -
Umyarov A.M.,
Rusina O.Yu.,
Gershanovitch V.N.
Publication year - 1986
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1986.tb01392.x
Subject(s) - pep group translocation , escherichia coli , phosphoenolpyruvate carboxykinase , biology , biochemistry , gene , enzyme , phosphotransferase , microbiology and biotechnology , genetics
The Escherichia coli ptsI and ptsH genes code for the synthesis of two proteins of the phosphoenolpyruvate‐dependent phosphotransferase system (PTS), namely enzyme I and protein HPr. A number of ptsI + ptsH + /F′ ptsI + ptsH merodiploids was obtained. It was shown in experiments in vivo that ptsH mutations in the transposition are dominant. Bacterial extracts from these merodiploids supported [ 14 C]methyl glucoside (MG) phosphorylation at the expense of phosphoenolpyruvate only half as much as extracts from the pts + cells. ptsI + ptsH /F′ ptsI + ptsH + merodiploids appeared to be non‐viable; the reason for this lack of viability is discussed.