PubAg

Main content area

Molecular mechanisms of RNA polymerase--the F/E (RPB4/7) complex is required for high processivity in vitro

Author:
Hirtreiter, Angela, Grohmann, Dina, Werner, Finn
Source:
Nucleic acids research 2010 v.38 no.2 pp. 585-596
ISSN:
0305-1048
Subject:
DNA-directed RNA polymerase, binding properties, messenger RNA, mutants
Abstract:
Transcription elongation in vitro is affected by the interactions between RNA polymerase (RNAP) subunits and the nucleic acid scaffold of the ternary elongation complex (TEC, RNAP-DNA-RNA). We have investigated the role of the RNAP subunits F/E (homologous to eukaryotic RPB4/7) during transcription elongation and termination using a wholly recombinant archaeal RNAP and synthetic nucleic acid scaffolds. The F/E complex greatly stimulates the processivity of RNAP, it enhances the formation of full length products, reduces pausing, and increases transcription termination facilitated by weak termination signals. Mutant variants of F/E that are defective in RNA binding show that these activities correlate with the nucleic acid binding properties of F/E. However, a second RNA-binding independent component also contributes to the stimulatory activities of F/E. In summary, our results suggest that interactions between RNAP subunits F/E and the RNA transcript are pivotal to the molecular mechanisms of RNAP during transcription elongation and termination.
Agid:
2229098