An alternative RNA polymerase I structure reveals a dimer hinge

Acta Crystallogr D Biol Crystallogr. 2015 Sep;71(Pt 9):1850-5. doi: 10.1107/S1399004715012651. Epub 2015 Aug 25.

Abstract

RNA polymerase I (Pol I) is the central, 14-subunit enzyme that synthesizes the ribosomal RNA (rRNA) precursor in eukaryotic cells. The recent crystal structure of Pol I at 2.8 Å resolution revealed two novel elements: the `expander' in the active-centre cleft and the `connector' that mediates Pol I dimerization [Engel et al. (2013), Nature (London), 502, 650-655]. Here, a Pol I structure in an alternative crystal form that was solved by molecular replacement using the original atomic Pol I structure is reported. The resulting alternative structure lacks the expander but still shows an expanded active-centre cleft. The neighbouring Pol I monomers form a homodimer with a relative orientation distinct from that observed previously, establishing the connector as a hinge between Pol I monomers.

Keywords: RNA polymerase I; connector; dimer; hinge.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Crystallography, X-Ray
  • Dimerization
  • Models, Molecular
  • Protein Conformation
  • RNA Polymerase I / chemistry*
  • Saccharomyces cerevisiae / enzymology*
  • Saccharomyces cerevisiae Proteins / chemistry*

Substances

  • Saccharomyces cerevisiae Proteins
  • RNA Polymerase I