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

Dmitry G. Vassylyev (), Shun-ichi Sekine, Oleg Laptenko, Jookyung Lee, Marina N. Vassylyeva, Sergei Borukhov and Shigeyuki Yokoyama
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Dmitry G. Vassylyev: RIKEN Harima Institute at Spring-8
Shun-ichi Sekine: 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
Sergei Borukhov: SUNY Health Science Center
Shigeyuki Yokoyama: RIKEN Harima Institute at Spring-8

Nature, 2002, vol. 417, issue 6890, 712-719

Abstract: 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.

Date: 2002
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DOI: 10.1038/nature752

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