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

Author

Listed:
  • Elizabeth A. Hubin

    (The Rockefeller University)

  • Mirjana Lilic

    (The Rockefeller University)

  • Seth A. Darst

    (The Rockefeller University)

  • Elizabeth A. Campbell

    (The Rockefeller University)

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.

Suggested Citation

  • Elizabeth A. Hubin & Mirjana Lilic & Seth A. Darst & Elizabeth A. Campbell, 2017. "Structural insights into the mycobacteria transcription initiation complex from analysis of X-ray crystal structures," Nature Communications, Nature, vol. 8(1), pages 1-12, December.
    • Handle: RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_ncomms16072
    DOI: 10.1038/ncomms16072
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    Cited by:

    1. Tomáš Kovaľ & Nabajyoti Borah & Petra Sudzinová & Barbora Brezovská & Hana Šanderová & Viola Vaňková Hausnerová & Alena Křenková & Martin Hubálek & Mária Trundová & Kristýna Adámková & Jarmila Dušková, 2024. "Mycobacterial HelD connects RNA polymerase recycling with transcription initiation," Nature Communications, Nature, vol. 15(1), pages 1-20, December.
    2. Reliza J. McGinnis & Chad A. Brambley & Brandon Stamey & William C. Green & Kimberly N. Gragg & Erin R. Cafferty & Thomas C. Terwilliger & Michal Hammel & Thomas J. Hollis & Justin M. Miller & Maria D, 2022. "A monomeric mycobacteriophage immunity repressor utilizes two domains to recognize an asymmetric DNA sequence," Nature Communications, Nature, vol. 13(1), pages 1-15, December.

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