Structural insights into the mycobacteria transcription initiation complex from analysis of X-ray crystal structures

Elizabeth A. Hubin, Mirjana Lilic, Seth A. Darst () and Elizabeth A. Campbell ()
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Elizabeth A. Hubin: The Rockefeller University
Mirjana Lilic: The Rockefeller University
Seth A. Darst: The Rockefeller University
Elizabeth A. Campbell: The Rockefeller University

Nature Communications, 2017, vol. 8, issue 1, 1-12

Abstract: Abstract The mycobacteria RNA polymerase (RNAP) is a target for antimicrobials against tuberculosis, motivating structure/function studies. Here we report a 3.2 Å-resolution crystal structure of a Mycobacterium smegmatis (Msm) open promoter complex (RPo), along with structural analysis of the Msm RPo and a previously reported 2.76 Å-resolution crystal structure of an Msm transcription initiation complex with a promoter DNA fragment. We observe the interaction of the Msm RNAP α-subunit C-terminal domain (αCTD) with DNA, and we provide evidence that the αCTD may play a role in Mtb transcription regulation. Our results reveal the structure of an Actinobacteria-unique insert of the RNAP β′ subunit. Finally, our analysis reveals the disposition of the N-terminal segment of Msm σA, which may comprise an intrinsically disordered protein domain unique to mycobacteria. The clade-specific features of the mycobacteria RNAP provide clues to the profound instability of mycobacteria RPo compared with E. coli.

Date: 2017
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DOI: 10.1038/ncomms16072

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