Structure of the 12-subunit RNA polymerase II refined with the aid of anomalous diffraction data.

ABSTRACT: RNA polymerase II (Pol II) is the central enzyme of eukaryotic gene expression machinery. Complete definition of the three-dimensional structure of Pol II is essential for understanding the mechanisms that regulate transcription via protein-protein interactions within the Pol II apparatus. To date a series of Pol II-related crystal structures have been reported. However, certain peptide regions, including several that are implicated to interact with regulatory factors, remain obscure. Here we describe conformations for two such regions that are close to the Pol II surface and assume seemingly flexible loop structures. One is located in the TFIIF-interacting Protrusion domain, whereas the other is in the TFIIE-interacting Clamp domain. This structural definition was aided by the application

SUBMITTER: Meyer PA 

PROVIDER: S-EPMC2676024 | biostudies-literature | 2009 May

REPOSITORIES: biostudies-literature