Lysine acetylation of DosR regulates the hypoxia response of Mycobacterium tuberculosis.

ABSTRACT: Tuberculosis caused by Mycobacterium tuberculosis (Mtb) infection remains a large global public health problem. One striking characteristic of Mtb is its ability to adapt to hypoxia and trigger the ensuing transition to a dormant state for persistent infection, but how the hypoxia response of Mtb is regulated remains largely unknown. Here we performed a quantitative acetylome analysis to compare the acetylation profile of Mtb under aeration and hypoxia, and showed that 377 acetylation sites in 269 Mtb proteins were significantly changed under hypoxia. In particular, deacetylation of dormancy survival regulator (DosR) at K182 promoted the hypoxia response in Mtb and enhanced the transcription of DosR-targeted genes. Mechanistically, recombinant DosR^K182R protein demonstrated enha

SUBMITTER: Yang H 

PROVIDER: S-EPMC5861037 | biostudies-literature | 2018 Mar

REPOSITORIES: biostudies-literature