Serine 83 in DosR,a response regulator from Mycobacterium tuberculosis, promotes its transition from an activated,phosphorylated state to an inactive,unphosphorylated state |
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Authors: | Ha Yeon Cho Beom Sik Kang |
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Institution: | School of Life Sciences and Biotechnology, Kyungpook National University, Daegu 702-701, Republic of Korea |
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Abstract: | A sensor kinase, DosS, and its corresponding response regulator, DosR, constitute a two component system for regulating gene expression under hypoxic conditions in Mycobacterium tuberculosis. Among response regulators in M. tuberculosis, NarL has high sequence similarity to DosR, and autophosphorylated DosS transfers its phosphate group not only to DosR but also to NarL. Phosphorylated DosR is more rapidly dephosphorylated than phosphorylated NarL. DosR and NarL differ with respect to the amino acids at positions T + 1 and T + 2 around the phosphorylation sites in the N-terminal phosphoacceptor domain; NarL has S83 and Y84, whereas DosR has A90 and H91. A DosR S83A mutant shows prolonged phosphorylation. Structural comparison with a histidinol phosphate phosphatase suggests that the hydroxyl group of DosR S83 could play a role in activating the water molecule involved in the triggering of autodephosphorylation. |
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Keywords: | TCS two component system HK histidine kinase RR response regulator REC domain receiving domain HAD haloacid dehydrogenase |
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