title: Molecular mechanisms of RNA polymerase--the F/E (RPB4/7) complex is required for high processivity in vitro.
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.
authors.affiliation: Division of Biosciences, Institute for Structural and Molecular Biology, University College London, Darwin Building, Gower Street, London WC1E 6BT, UK.
authors.forename: Angela
authors.initials: A
authors.lastname: Hirtreiter
authors.forename: Dina
authors.initials: D
authors.lastname: Grohmann
authors.forename: Finn
authors.initials: F
authors.lastname: Werner
mesh_terms: D019843:Archaeal Proteins / Q000737:chemistry / Q000378:metabolism*; D004247:DNA / Q000378:metabolism; D012321:DNA-Directed RNA Polymerases / Q000737:chemistry / Q000378:metabolism*; D011072:Poly U / Q000737:chemistry; D021122:Protein Subunits / Q000737:chemistry / Q000378:metabolism; D014158:Transcription, Genetic
chemical_list: D019843:Archaeal Proteins; D021122:Protein Subunits; D011072:Poly U; D004247:DNA; D012321:DNA-Directed RNA Polymerases