Premium
A novel two‐component system found in Mycobacterium tuberculosis
Author(s) -
Morth J. Preben,
Gosmann Sylvi,
Nowak Elzbieta,
Tucker Paul A.
Publication year - 2005
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2005.06.043
Subject(s) - two component regulatory system , response regulator , mycobacterium tuberculosis , antitermination , kinase , histidine kinase , phosphorylation , biology , mycobacterium , chemistry , regulator , component (thermodynamics) , locus (genetics) , histidine , biochemistry , tuberculosis , computational biology , microbiology and biotechnology , genetics , operon , bacteria , gene , bacterial protein , enzyme , medicine , physics , pathology , escherichia coli , mutant , thermodynamics
We report the identification of a novel two‐component system in Mycobacterium tuberculosis. We show that the putative histidine kinase with the genomic locus tag Rv3220c is able to self‐phosphorylate in the presence of Mg 2+ /ATP and subsequently transfer the phosphoryl group to a novel response regulator PdtaR. This creates a biochemical link between the two proteins and establishes a newly identified two component system, which acts at the level of transcriptional antitermination. We also suggest that this system has potential for the development of lead compounds for inhibition of phosphotransfer.