Abstract:
:PhoR of Bacillus subtilis is a histidine sensor-kinase belonging to the family of two-component signal transduction systems. PhoR is responsible for processing the phosphate-starvation signal and providing phosphate input to regulate the level of phosphorylated response regulator, PhoP, which activates/represses Pho regulon gene transcription. The catalytic domain of PhoR is sufficient for the low-phosphate inducible expression of Pho regulon genes since removing the N-terminal membrane-associated domain did not alter the kinetics of Pho induction, albeit the total level of induction was decreased (1). In this study we showed that the complete B. subtilis PhoR protein produced in Escherichia coli can be reverse phosphorylated by PhoP-phosphate. We also used a C-terminal fragment of the PhoR protein, PhoR, to demonstrate that the phosphoryl group on phospho-PhoP was transferred back to PhoR in the reverse phosphorylation reaction or released as inorganic phosphate to the reaction mixture. The reverse phosphorylation of the PhoR protein likely occurs at the same histidine residue (His360) that is utilized for the autokinase reaction by the same protein. In the presence of ADP, the phosphoryl group is further transferred to ADP to form ATP. While the autokinase reaction, the forward phosphotransfer reaction from PhoR approximately P to PhoP, and the release of inorganic phosphate from PhoP approximately P in the presence of PhoR require Mg(2+), the reverse phosphotransfer from PhoP approximately P to PhoR does not. These results indicate that the energy levels of the phosphoryl groups on PhoP and PhoR are very similar. The reversible autokinase reaction and/or the reversible phosphotransfer reaction between PhoR approximately P and PhoP may have a role in PhoP approximately P decay thus influencing the PhoP approximately P concentration in the cell.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Shi L,Liu W,Hulett FMdoi
10.1021/bi990658tsubject
Has Abstractpub_date
1999-08-03 00:00:00pages
10119-25issue
31eissn
0006-2960issn
1520-4995pii
bi990658tjournal_volume
38pub_type
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