Structure of the complete elongation complex of RNA polymerase II with basal factors

Science. 2017 Sep 1;357(6354):921-924. doi: 10.1126/science.aan8552. Epub 2017 Aug 3.

Abstract

In the early stage of transcription, eukaryotic RNA polymerase II (Pol II) exchanges initiation factors with elongation factors to form an elongation complex for processive transcription. Here we report the structure of the Pol II elongation complex bound with the basal elongation factors Spt4/5, Elf1, and TFIIS. Spt4/5 (the Spt4/Spt5 complex) and Elf1 modify a wide area of the Pol II surface. Elf1 bridges the Pol II central cleft, completing a "DNA entry tunnel" for downstream DNA. Spt4 and the Spt5 NGN and KOW1 domains encircle the upstream DNA, constituting a "DNA exit tunnel." The Spt5 KOW4 and KOW5 domains augment the "RNA exit tunnel," directing the exiting nascent RNA. Thus, the elongation complex establishes a completely different transcription and regulation platform from that of the initiation complexes.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / ultrastructure
  • Cryoelectron Microscopy
  • Crystallography, X-Ray
  • Klebsiella / enzymology*
  • Protein Domains
  • RNA Polymerase II / chemistry*
  • RNA Polymerase II / ultrastructure
  • RNA, Messenger / biosynthesis*
  • Transcription Elongation, Genetic*
  • Transcription Factors / chemistry*
  • Transcription Factors / ultrastructure

Substances

  • Bacterial Proteins
  • RNA, Messenger
  • Transcription Factors
  • RNA Polymerase II