Crystal structure of RPB5, a universal eukaryotic RNA polymerase subunit and transcription factor interaction target

Proc Natl Acad Sci U S A. 2000 Jun 6;97(12):6306-10. doi: 10.1073/pnas.97.12.6306.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • DNA-Directed RNA Polymerases / chemistry*
  • Dimerization
  • Molecular Sequence Data
  • Protein Structure, Secondary
  • Saccharomyces cerevisiae / enzymology*


  • DNA-Directed RNA Polymerases

Associated data

  • PDB/1DZF