Publication Abstract from PubMed
Eukaryotic nuclei contain three different types of RNA polymerases (RNAPs), each consisting of 12-18 different subunits. The evolutionarily highly conserved RNAP subunit RPB5 is shared by all three enzymes and therefore represents a key structural/functional component of all eukaryotic RNAPs. Here we present the crystal structure of the RPB5 subunit from Saccharomyces cerevisiae. The bipartite structure includes a eukaryote-specific N-terminal domain and a C-terminal domain resembling the archaeal RNAP subunit H. RPB5 has been implicated in direct protein-protein contacts with transcription factor IIB, one of the components of the RNAP(II) basal transcriptional machinery, and gene-specific activator proteins, such as the hepatitis B virus transactivator protein X. The experimentally mapped regions of RPB5 involved in these interactions correspond to distinct and surface-exposed alpha-helical structures.
Crystal structure of RPB5, a universal eukaryotic RNA polymerase subunit and transcription factor interaction target.,Todone F, Weinzierl RO, Brick P, Onesti S Proc Natl Acad Sci U S A. 2000 Jun 6;97(12):6306-10. PMID:10841537[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
