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"TFIIH XPB mutants suggest a unified bacterial-like mechanism for promoter opening but not escape." |
Lin YC, Choi WS, Gralla JD. |
Published July 1, 2005 in Nat Struct Mol Biol. volume 12 .
Pubmed ID: 15937491
Abstract:
| DNA helicases open the duplex during DNA replication, repair and transcription. However, RNA polymerase II is the only member of its family with this requirement; RNA polymerases I and III and bacterial RNA polymerases open DNA without a helicase. In this report, characterization of XPB mutants indicates that its helicase activity is not used for RNA polymerase II promoter opening, which is instead driven by its ATPase activity. The mutants have parallels in sigma(54) bacterial transcription and this suggests a similar mode of opening DNA for both RNA polymerases, involving ATP-dependent enzyme conformational changes. Promoter escape is defective in these XPB mutants, suggesting that the XPB helicase acts as an ATP-driven motor to reorganize the tightly wrapped multiprotein eukaryotic preinitiation complex during the remodeling that precedes elongation and the coupling to RNA processing events. |
This publication refers to following REPAIRtoire entries:
| Pathways |
Last modification of this entry: Dec. 10, 2008
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