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

Hubin, Elizabeth A.; Lilic, Mirjana; Darst, Seth A.; Campbell, Elizabeth A.

doi:10.1038/ncomms16072

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

Journal Article · Thu Jul 13 00:00:00 EDT 2017 · Nature Communications

DOI: https://doi.org/10.1038/ncomms16072 · OSTI ID:1393440

Hubin, Elizabeth A. ^[1]; Lilic, Mirjana ^[2]; Darst, Seth A. ^[2]; Campbell, Elizabeth A. ^[2]

Rockefeller Univ., New York, NY (United States); The Rockefeller University, 1230 York Avenue, New York, New York
Rockefeller Univ., New York, NY (United States)

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 a CTD may play a role in Mtb transcription regulation. Here, 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 σ^A, 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.

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Research Organization:: Univ. of Chicago, IL (United States)

Sponsoring Organization:: USDOE Office of Science (SC); National Institutes of Health (NIH)

Grant/Contract Number:: AC02-06CH11357

OSTI ID:: 1393440

Journal Information:: Nature Communications, Journal Name: Nature Communications Vol. 8; ISSN 2041-1723

Publisher:: Nature Publishing GroupCopyright Statement

Country of Publication:: United States

Language:: English

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CarD and RbpA modify the kinetics of initial transcription and slow promoter escape of the Mycobacterium tuberculosis RNA polymerase Jensen, Drake; Manzano, Ana Ruiz; Rammohan, Jayan Nucleic Acids Research, Vol. 47, Issue 13 https://doi.org/10.1093/nar/gkz449	journal	May 2019
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Structural basis of non-canonical transcriptional regulation by the σA-bound iron-sulfur protein WhiB1 in M. tuberculosis Wan, Tao; Li, Shanren; Beltran, Daisy Guiza Nucleic Acids Research, Vol. 48, Issue 2 https://doi.org/10.1093/nar/gkz1133	journal	December 2019
CarD and RbpA modify the kinetics of initial transcription and slow promoter escape of the Mycobacterium tuberculosis RNA polymerase Jensen, Drake; Manzano, Ana Ruiz; Rammohan, Jayan Nucleic Acids Research, Vol. 47, Issue 13 https://doi.org/10.1093/nar/gkz449	journal	May 2019
The Core and Holoenzyme Forms of RNA Polymerase from Mycobacterium smegmatis Kouba, Tomáš; Pospíšil, Jiří; Hnilicová, Jarmila Journal of Bacteriology, Vol. 201, Issue 4 https://doi.org/10.1128/jb.00583-18	journal	November 2018
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Fidaxomicin jams Mycobacterium tuberculosis RNA polymerase motions needed for initiation via RbpA contacts Boyaci, Hande; Chen, James; Lilic, Mirjana eLife, Vol. 7 https://doi.org/10.7554/elife.34823	journal	February 2018
E. coli TraR allosterically regulates transcription initiation by altering RNA polymerase conformation Chen, James; Gopalkrishnan, Saumya; Chiu, Courtney eLife, Vol. 8 https://doi.org/10.7554/elife.49375	journal	December 2019

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