Architecture of the RNA polymerase-Spt4/5 complex and basis of universal transcription processivity
Open Access
- 8 March 2011
- journal article
- Published by Springer Science and Business Media LLC in The EMBO Journal
- Vol. 30 (7), 1302-1310
- https://doi.org/10.1038/emboj.2011.64
Abstract
Related RNA polymerases (RNAPs) carry out cellular gene transcription in all three kingdoms of life. The universal conservation of the transcription machinery extends to a single RNAP‐associated factor, Spt5 (or NusG in bacteria), which renders RNAP processive and may have arisen early to permit evolution of long genes. Spt5 associates with Spt4 to form the Spt4/5 heterodimer. Here, we present the crystal structure of archaeal Spt4/5 bound to the RNAP clamp domain, which forms one side of the RNAP active centre cleft. The structure revealed a conserved Spt5–RNAP interface and enabled modelling of complexes of Spt4/5 counterparts with RNAPs from all kingdoms of life, and of the complete yeast RNAP II elongation complex with bound Spt4/5. The N‐terminal NGN domain of Spt5/NusG closes the RNAP active centre cleft to lock nucleic acids and render the elongation complex stable and processive. The C‐terminal KOW1 domain is mobile, but its location is restricted to a region between the RNAP clamp and wall above the RNA exit tunnel, where it may interact with RNA and/or other factors.Keywords
This publication has 62 references indexed in Scilit:
- Structure of an RNA Polymerase II–TFIIB Complex and the Transcription Initiation MechanismScience, 2010
- Phosphorylation of the Transcription Elongation Factor Spt5 by Yeast Bur1 Kinase Stimulates Recruitment of the PAF ComplexMolecular and Cellular Biology, 2009
- Structural Basis of Transcription: Mismatch-Specific Fidelity Mechanisms and Paused RNA Polymerase II with Frayed RNAMolecular Cell, 2009
- Core Structure of the Yeast Spt4-Spt5 Complex: A Conserved Module for Regulation of Transcription ElongationStructure, 2008
- The elongation factor RfaH and the initiation factor σ bind to the same site on the transcription elongation complexProceedings of the National Academy of Sciences of the United States of America, 2008
- The positions of TFIIF and TFIIE in the RNA polymerase II transcription preinitiation complexNature Structural & Molecular Biology, 2007
- Electrostatics of nanosystems: Application to microtubules and the ribosomeProceedings of the National Academy of Sciences of the United States of America, 2001
- Spt4 modulates Rad26 requirement in transcription-coupled nucleotide excision repairThe EMBO Journal, 2000
- Crystal Structure of Thermus aquaticus Core RNA Polymerase at 3.3 Å ResolutionCell, 1999
- Evidence that Spt4, Spt5, and Spt6 control transcription elongation by RNA polymerase II in Saccharomyces cerevisiaeJournal of Bone and Joint Surgery, 1998