IDEAS home Printed from https://ideas.repec.org/a/nat/natcom/v8y2017i1d10.1038_ncomms16072.html
   My bibliography  Save this article

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
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/ncomms16072
    File Function: Abstract
    Download Restriction: no
    File URL: https://libkey.io/10.1038/ncomms16072?utm_source=ideas
    LibKey link: if access is restricted and if your library uses this service, LibKey will redirect you to where you can use your library subscription to access this item
    ---><---

    Citations

    Citations are extracted by the CitEc Project, subscribe to its RSS feed for this item.
    as


    Cited by:

    1. 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.

    More about this item

    Statistics

    Access and download statistics

    Corrections

    All material on this site has been provided by the respective publishers and authors. You can help correct errors and omissions. When requesting a correction, please mention this item's handle: RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_ncomms16072. See general information about how to correct material in RePEc.

    If you have authored this item and are not yet registered with RePEc, we encourage you to do it here. This allows to link your profile to this item. It also allows you to accept potential citations to this item that we are uncertain about.

    We have no bibliographic references for this item. You can help adding them by using this form .

    If you know of missing items citing this one, you can help us creating those links by adding the relevant references in the same way as above, for each refering item. If you are a registered author of this item, you may also want to check the "citations" tab in your RePEc Author Service profile, as there may be some citations waiting for confirmation.

    For technical questions regarding this item, or to correct its authors, title, abstract, bibliographic or download information, contact: Sonal Shukla or Springer Nature Abstracting and Indexing (email available below). General contact details of provider: http://www.nature.com .

    Please note that corrections may take a couple of weeks to filter through the various RePEc services.

    IDEAS is a RePEc service. RePEc uses bibliographic data supplied by the respective publishers.