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Crystal structure of a bacterial RNA polymerase holoenzyme at 2.6 Å resolution

Author

Listed:
  • Dmitry G. Vassylyev

    (RIKEN Harima Institute at Spring-8
    RIKEN Harima Institute at Spring-8)

  • Shun-ichi Sekine

    (RIKEN Harima Institute at Spring-8
    RIKEN Harima Institute at Spring-8)

  • Oleg Laptenko

    (SUNY Health Science Center)

  • Jookyung Lee

    (SUNY Health Science Center)

  • Marina N. Vassylyeva

    (RIKEN Harima Institute at Spring-8
    RIKEN Genomic Sciences Center)

  • Sergei Borukhov

    (SUNY Health Science Center)

  • Shigeyuki Yokoyama

    (RIKEN Harima Institute at Spring-8
    RIKEN Harima Institute at Spring-8
    RIKEN Genomic Sciences Center
    University of Tokyo)

Abstract

In bacteria, the binding of a single protein, the initiation factor σ, to a multi-subunit RNA polymerase core enzyme results in the formation of a holoenzyme, the active form of RNA polymerase essential for transcription initiation. Here we report the crystal structure of a bacterial RNA polymerase holoenzyme from Thermus thermophilus at 2.6 Å resolution. In the structure, two amino-terminal domains of the σ subunit form a V-shaped structure near the opening of the upstream DNA-binding channel of the active site cleft. The carboxy-terminal domain of σ is near the outlet of the RNA-exit channel, about 57 Å from the N-terminal domains. The extended linker domain forms a hairpin protruding into the active site cleft, then stretching through the RNA-exit channel to connect the N- and C-terminal domains. The holoenzyme structure provides insight into the structural organization of transcription intermediate complexes and into the mechanism of transcription initiation.

Suggested Citation

  • Dmitry G. Vassylyev & Shun-ichi Sekine & Oleg Laptenko & Jookyung Lee & Marina N. Vassylyeva & Sergei Borukhov & Shigeyuki Yokoyama, 2002. "Crystal structure of a bacterial RNA polymerase holoenzyme at 2.6 Å resolution," Nature, Nature, vol. 417(6890), pages 712-719, June.
    • Handle: RePEc:nat:nature:v:417:y:2002:i:6890:d:10.1038_nature752
    DOI: 10.1038/nature752
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    Cited by:

    1. Zakia Morichaud & Stefano Trapani & Rishi K. Vishwakarma & Laurent Chaloin & Corinne Lionne & Joséphine Lai-Kee-Him & Patrick Bron & Konstantin Brodolin, 2023. "Structural basis of the mycobacterial stress-response RNA polymerase auto-inhibition via oligomerization," Nature Communications, Nature, vol. 14(1), pages 1-13, December.
    2. Dingwei He & Linlin You & Xiaoxian Wu & Jing Shi & Aijia Wen & Zhi Yan & Wenhui Mu & Chengli Fang & Yu Feng & Yu Zhang, 2022. "Pseudomonas aeruginosa SutA wedges RNAP lobe domain open to facilitate promoter DNA unwinding," Nature Communications, Nature, vol. 13(1), pages 1-10, December.

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