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PMID: 21386817 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Architecture of the RNA polymerase-Spt4/5 complex and basis of universal transcription processivity.

The EMBO journal ·Vol. 30 ·No. 7 ·2011-04-06 ·Pages 1302-10

Martinez-Rucobo FW, Sainsbury S, Cheung AC, Cramer P

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.

MeSH Terms
Amino Acid Sequence Chromosomal Proteins, Non-Histone/chemistry Crystallography, X-Ray DNA-Directed RNA Polymerases/chemistry Models, Molecular Molecular Sequence Data Protein Binding Protein Structure, Quaternary Pyrococcus furiosus/chemistry,enzymology Repressor Proteins/chemistry Saccharomyces cerevisiae/chemistry,enzymology Sequence Homology, Amino Acid Transcriptional Elongation Factors/chemistry
Chemicals
Chromosomal Proteins, Non-Histone Repressor Proteins Transcriptional Elongation Factors SPT5 transcriptional elongation factor DNA-Directed RNA Polymerases
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Martinez-Rucobo Fuensanta W
Gene Center and Department of Biochemistry, Center for Integrated Protein Science Munich (CIPSM), Ludwig-Maximilians-Universität München, Munich, Germany.
Sainsbury Sarah
Cheung Alan C M
Cramer Patrick
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Article Info
Journal
The EMBO journal
Abbr.
EMBO J
ISSN
1460-2075
DOI
10.1038/emboj.2011.64
Published
2011-04-06
Epub
2011-00-08
Pages
1302-10
Language
English
Region
England
NLM ID
8208664
PMCID
PMC3094117
Subset
IM
Databases
PDB
3QQC
Corrections
CommentIn
PMID: 21468097
CommentIn
PMID: 21777806
External Links
PubMed source DOI: 10.1038/emboj.2011.64 PMC Full Text View journal details
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