Architecture of the RNA polymerase-Spt4/5 complex and basis of universal transcription processivity
EMBO Journal, ISSN: 0261-4189, Vol: 30, Issue: 7, Page: 1302-1310
2011
- 204Citations
- 180Captures
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Metrics Details
- Citations204
- Citation Indexes204
- CrossRef204
- 197
- Captures180
- Readers180
- 180
Article Description
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. © 2011 European Molecular Biology Organization. All Rights Reserved.
Bibliographic Details
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=79953779997&origin=inward; http://dx.doi.org/10.1038/emboj.2011.64; http://www.ncbi.nlm.nih.gov/pubmed/21386817; http://emboj.embopress.org/cgi/doi/10.1038/emboj.2011.64; https://dx.doi.org/10.1038/emboj.2011.64; https://www.embopress.org/doi/full/10.1038/emboj.2011.64
Springer Science and Business Media LLC
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