Structural Basis of Transcription Initiation: An RNA Polymerase Holoenzyme-DNA Complex
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- 17 May 2002
- journal article
- research article
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 296 (5571) , 1285-1290
- https://doi.org/10.1126/science.1069595
Abstract
The crystal structure ofThermus aquaticusRNA polymerase holoenzyme (α2ββ′ωσA) complexed with a fork-junction promoter DNA fragment has been determined by fitting high-resolution x-ray structures of individual components into a 6.5-angstrom resolution map. The DNA lies across one face of the holoenzyme, completely outside the RNA polymerase active site channel. All sequence-specific contacts with core promoter elements are mediated by the σ subunit. A universally conserved tryptophan is ideally positioned to stack on the exposed face of the base pair at the upstream edge of the transcription bubble. Universally conserved basic residues of the σ subunit provide critical contacts with the DNA phosphate backbone and play a role in directing the melted DNA template strand into the RNA polymerase active site. The structure explains how holoenzyme recognizes promoters containing variably spaced –10 and –35 elements and provides the basis for models of the closed and open promoter complexes.Keywords
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