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Research Article

The Core and Holoenzyme Forms of RNA Polymerase from Mycobacterium smegmatis

Tomáš Kouba, Jiří Pospíšil, Jarmila Hnilicová, Hana Šanderová, Ivan Barvík, Libor Krásný
Ann M. Stock, Editor
Tomáš Kouba
MRC Laboratory of Molecular Biology, Cambridge, United Kingdom
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Jiří Pospíšil
Laboratory of Microbial Genetics and Gene Expression, Institute of Microbiology, Academy of Sciences of the Czech Republic, Prague, Czech RepublicDepartment of Genetics and Microbiology, Faculty of Science, Charles University in Prague, Prague, Czech Republic
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Jarmila Hnilicová
Laboratory of Microbial Genetics and Gene Expression, Institute of Microbiology, Academy of Sciences of the Czech Republic, Prague, Czech Republic
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Hana Šanderová
Laboratory of Microbial Genetics and Gene Expression, Institute of Microbiology, Academy of Sciences of the Czech Republic, Prague, Czech Republic
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Ivan Barvík
Division of Biomolecular Physics, Institute of Physics, Faculty of Mathematics and Physics, Charles University in Prague, Prague, Czech Republic
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Libor Krásný
Laboratory of Microbial Genetics and Gene Expression, Institute of Microbiology, Academy of Sciences of the Czech Republic, Prague, Czech Republic
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  • ORCID record for Libor Krásný
Ann M. Stock
Rutgers University-Robert Wood Johnson Medical School
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DOI: 10.1128/JB.00583-18
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ABSTRACT

Bacterial RNA polymerase (RNAP) is essential for gene expression and as such is a valid drug target. Hence, it is imperative to know its structure and dynamics. Here, we present two as-yet-unreported forms of Mycobacterium smegmatis RNAP: core and holoenzyme containing σA but no other factors. Each form was detected by cryo-electron microscopy in two major conformations. Comparisons of these structures with known structures of other RNAPs reveal a high degree of conformational flexibility of the mycobacterial enzyme and confirm that region 1.1 of σA is directed into the primary channel of RNAP. Taken together, we describe the conformational changes of unrestrained mycobacterial RNAP.

IMPORTANCE We describe here three-dimensional structures of core and holoenzyme forms of mycobacterial RNA polymerase (RNAP) solved by cryo-electron microscopy. These structures fill the thus-far-empty spots in the gallery of the pivotal forms of mycobacterial RNAP and illuminate the extent of conformational dynamics of this enzyme. The presented findings may facilitate future designs of antimycobacterial drugs targeting RNAP.

FOOTNOTES

    • Received 20 September 2018.
    • Accepted 20 November 2018.
    • Accepted manuscript posted online 26 November 2018.
  • Supplemental material for this article may be found at https://doi.org/10.1128/JB.00583-18.

  • Copyright © 2019 American Society for Microbiology.

All Rights Reserved.

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The Core and Holoenzyme Forms of RNA Polymerase from Mycobacterium smegmatis
Tomáš Kouba, Jiří Pospíšil, Jarmila Hnilicová, Hana Šanderová, Ivan Barvík, Libor Krásný
Journal of Bacteriology Jan 2019, 201 (4) e00583-18; DOI: 10.1128/JB.00583-18

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The Core and Holoenzyme Forms of RNA Polymerase from Mycobacterium smegmatis
Tomáš Kouba, Jiří Pospíšil, Jarmila Hnilicová, Hana Šanderová, Ivan Barvík, Libor Krásný
Journal of Bacteriology Jan 2019, 201 (4) e00583-18; DOI: 10.1128/JB.00583-18
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KEYWORDS

RNA polymerase
bacterial transcription
conformational change
cryo-electron microscopy
mycobacteria
protein structure
transcription initiation factor

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