Open AccessGenetic and Biochemical Studies of Phosphatase Activity of PhoR
Author(s) -
Daniel Carmany,
Kristine Hollingsworth,
William R. McCleary
Publication year - 2003
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.185.3.1112-1115.2003
Subject(s) - regulon , biology , histidine , phosphatase , histidine kinase , phosphorylation , escherichia coli , mutant , biochemistry , function (biology) , genetics , enzyme , gene
In Escherichia coli, PhoR is the histidine kinase of the phosphate regulon. It has been postulated that PhoR may function as a phospho-PhoB phosphatase. Experiments with four precise phoR deletion mutants supported this hypothesis and suggested that this activity resides within the histidine phosphorylation domain. This biochemical activity was confirmed by using a separately expressed histidine phosphorylation domain.