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The Mycobacterium tuberculosis transcriptional repressor EthR is negatively regulated by Serine/Threonine phosphorylation.

Abstract：

:Recent efforts have underlined the role of Serine/Threonine Protein Kinases (STPKs) in growth, pathogenesis and cell wall metabolism in mycobacteria. Herein, we demonstrated that the Mycobacterium tuberculosis EthR, a transcriptional repressor that regulates the activation process of the antitubercular drug ethionamide (ETH) is a specific substrate of the mycobacterial kinase PknF. ETH is a prodrug that must undergo bioactivation by the monooxygenease EthA to exert its antimycobacterial activity and previous studies reported that EthR represses transcription of ethA by binding to the ethA-ethR intergenic region. Mass spectrometry analyses and site-directed mutagenesis identified a set of four phosphoacceptors, namely Thr2, Thr3, Ser4 and Ser7. This was further supported by the complete loss of PknF-dependent phosphorylation of a phosphoablative EthR mutant protein. Importantly, a phosphomimetic version of EthR, in which all phosphosites were replaced by Asp residues, exhibited markedly decreased DNA-binding activity compared with the wild-type protein. Together, these findings are the first demonstration of EthR phosphorylation and indicate that phosphorylation negatively affects its DNA-binding activity, which may impact ETH resistance levels in M. tb.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Leiba J,Carrère-Kremer S,Blondiaux N,Dimala MM,Wohlkönig A,Baulard A,Kremer L,Molle V

doi

10.1016/j.bbrc.2014.03.074

subject

Has Abstract

pub_date

2014-04-18 00:00:00

pages

1132-8

issue

4

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(14)00517-8

journal_volume

446

pub_type

杂志文章

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