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Phosphotransfer signal transduction between two regulatory factors involved in the osmoregulated kdp operon in Escherichia coli
Author(s) -
Nakashima K.,
Sugiura A.,
Momoi H.,
Mizuno T.
Publication year - 1992
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.1992.tb01350.x
Subject(s) - operon , biology , autophosphorylation , escherichia coli , phosphorylation , signal transduction , biochemistry , microbiology and biotechnology , gene , protein kinase a
Summary The proteins KdpD and KdpE are regulatory factors critically involved in the osmotic regulation of the kdpABC operon that is responsible for a high‐affinity transport system in Escherichia coli. In this study, we obtained biochemical evidence supporting the view that the KdpD protein is a sensory protein kinase that exhibits autophosphorylation and KdpE‐phosphotransfer characteristics. During the course of such studies we established a procedure for purifying the KdpE protein in large quantities. We also developed a procedure for preparing cytoplasmic membrane enriched with the KdpD protein that exhibits in vitro ability with regard to phosphorylation of KdpE protein.