Formation and crystallization of yeast RNA polymerase II elongation complexes

J Biol Chem. 1997 Dec 5;272(49):30799-805. doi: 10.1074/jbc.272.49.30799.

Abstract

Minimal templates were devised for the efficient generation of yeast RNA polymerase II transcription elongation complexes. A 33-base pair DNA with a 15-residue dC tail at one 3'-end supported the formation of a complex containing the polymerase paused at nucleotide 11 of the duplex region and an RNA of 14-16 residues. The same template could yield an arrested complex with the enzyme at nucleotide 13-15 and RNA of 15-17 residues. These complexes were stable for at least a week under various conditions and could be resolved by gel electrophoresis or purified by ion exchange chromatography. The purified paused complex formed crystals capable of x-ray diffraction to 3.5 A resolution. The complex remained active in the crystal and, in the presence of nucleoside triphosphates, could efficiently extend the transcript in situ.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Base Sequence
  • Crystallography, X-Ray
  • DNA / chemistry
  • DNA / metabolism
  • Molecular Sequence Data
  • Peptide Chain Elongation, Translational*
  • Protein Conformation
  • RNA Polymerase II / chemistry*
  • RNA Polymerase II / metabolism
  • Saccharomyces cerevisiae
  • Templates, Genetic
  • Transcription Factors / chemistry
  • Transcription Factors / metabolism
  • Transcription Factors, General*
  • Transcription, Genetic
  • Transcriptional Elongation Factors*

Substances

  • Transcription Factors
  • Transcription Factors, General
  • Transcriptional Elongation Factors
  • transcription factor S-II
  • DNA
  • RNA Polymerase II