Importance of the α10 helix for DevR activation: A road map for screening inhibitors against DevR-mediated dormancy of Mycobacterium tuberculosis | Zendy

Atul Vashist | Zendy; Dinesh Raj | Zendy; Umesh Datta Gupta | Zendy; Rajiv Bhat | Zendy; Jaya Sivaswami Tyagi | Zendy

Open Access

Importance of the α10 helix for DevR activation: A road map for screening inhibitors against DevR-mediated dormancy of Mycobacterium tuberculosis

Author(s) -

Atul Vashist,

Dinesh Raj,

Umesh Datta Gupta,

Rajiv Bhat,

Jaya Sivaswami Tyagi

Publication year - 2016

Publication title -

international journal of mycobacteriology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.53

H-Index - 20

eISSN - 2212-554X

pISSN - 2212-5531

DOI - 10.1016/j.ijmyco.2016.09.030

Subject(s) - electrophoretic mobility shift assay , mycobacterium tuberculosis , regulon , biology , mutant , circular dichroism , binding site , response regulator , tetr , transcription factor , biochemistry , gene , tuberculosis , repressor , medicine , pathology

Bacterial persistence is the hallmark of tuberculosis (TB) and poses the biggest threat to the success of any antitubercular drug regimen. The DevR/DosR dormancy regulator of Mycobacterium tuberculosis belongs to the NarL subfamily of response regulators and is essential for M. tuberculosis persistence in macaque models of TB. The DevR/DosR crystal structure revealed a unique (αβ) 4 opology instead of the classical (αβ) 5 structure found in the receiver domain of other regulators in this subfamily. It was proposed that phosphorylation may culminate in the formation of a DNA-binding-competent dimeric species via α10-α10 helix interactions. Here, we deciphered the role of the α10 helix in activation of the DevR/DosR response regulator in M. tuberculosis.

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