Structure of the yeast RNA polymerase II holoenzyme: Mediator conformation and polymerase interaction.
The holoenzyme formed by RNA polymerase II (RNAPII) and the Mediator complex is the target of transcriptional regulators in vivo. A three-dimensional structure of the yeast holoenzyme has been generated from electron microscopic images of single holoenzyme particles. Extensive changes in Mediator conformation required for interaction with RNAPII have been modeled by correlating the polymerase-bound and free Mediator structures. Determination of the precise orientation of the RNAPII in the holoenzyme indicates that Mediator contacts are centered on the RNAPII Rpb3/Rpb11 heterodimer, the eukaryotic homolog of the alpha(2) homodimer involved in transcription regulation in prokaryotes. Implications for the possible mechanism of transcription regulation by Mediator are discussed.
Department of Cell Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.
Joshua A
JA
Davis
Yuichiro
Y
Takagi
Roger D
RD
Kornberg
Francisco A
FA
Asturias
D001665:Binding Sites; D020035:Holoenzymes / Q000737:chemistry* / Q000378:metabolism* / Q000648:ultrastructure; D046911:Macromolecular Substances; D008854:Microscopy, Electron; D008958:Models, Molecular; D011485:Protein Binding; D020836:Protein Structure, Quaternary; D012319:RNA Polymerase II / Q000737:chemistry* / Q000378:metabolism* / Q000648:ultrastructure; D012441:Saccharomyces cerevisiae / Q000201:enzymology*
D020035:Holoenzymes; D046911:Macromolecular Substances; D012319:RNA Polymerase II