Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Target Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Query: EC:2.7.13.3 (
histidine kinase
)
2,405
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
Gluconobacter oxydans may contain an incomplete phosphoenolpyruvate: carbohydrate phosphotransferase system consisting of three components--EI, HPr and EIIA, while the function of individual members of the system remains unknown. In this research, a specific interaction between EI and a
histidine kinase
-response regulator hybrid protein was screened by yeast two-hybrid assay, and the interaction was further identified with GST pull-down assay and bimolecular fluorescence complementation assay in vitro and in vivo, respectively. As the
histidine kinase
-response regulator hybrid protein serves as a member of two-component system in G. oxydans, its interaction with EI implied that
PTS
may play certain roles in bacteria under stress.
...
PMID:Identification of an interaction between EI and a histidine kinase-response regulator hybrid protein in Gluconobacter oxydans. 2679 29
SixA, a well-conserved protein found in proteobacteria, actinobacteria, and cyanobacteria, is the only reported example of a bacterial phosphohistidine phosphatase. A single protein target of SixA has been reported to date: the
Escherichia coli
histidine kinase
ArcB. The present work analyzes an ArcB-independent growth defect of a
sixA
deletion in
E. coli
A screen for suppressors, analysis of various mutants, and phosphorylation assays indicate that SixA modulates phosphorylation of the nitrogen-related phosphotransferase system (
PTS
Ntr
). The
PTS
Ntr
is a widely conserved bacterial pathway that regulates diverse metabolic processes through the phosphorylation states of its protein components, EI
Ntr
, NPr, and EIIA
Ntr
, which receive phosphoryl groups on histidine residues. However, a mechanism for dephosphorylating this system has not been reported. The results presented here suggest a model in which SixA removes phosphoryl groups from the
PTS
Ntr
by acting on NPr. This work uncovers a new role for the phosphohistidine phosphatase SixA and, through factors that affect SixA expression or activity, may point to additional inputs that regulate the
PTS
Ntr
IMPORTANCE
One common means to regulate protein activity is through phosphorylation. Protein phosphatases exist to reverse this process, returning the protein to the unphosphorylated form. The vast majority of protein phosphatases that have been identified target phosphoserine, phosphotheronine, and phosphotyrosine. A widely conserved phosphohistidine phosphatase was identified in
Escherichia coli
20 years ago but remains relatively understudied. The present work shows that this phosphatase modulates the nitrogen-related phosphotransferase system, a pathway that is regulated by nitrogen and carbon metabolism and affects diverse aspects of bacterial physiology. Until now, there was no known mechanism for removing phosphoryl groups from this pathway.
...
PMID:The Phosphohistidine Phosphatase SixA Targets a Phosphotransferase System. 3048 31
