ArticleThe EMBO journal2011
Architecture of the RNA polymerase-Spt4/5 complex and basis of universal transcription processivity.
Article in The EMBO journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 152 papers.
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Who cites it
152 citing papers in PubMed, 237 citations in OpenAlex.
- DSIF factor Spt5 coordinates transcription, maturation and exoribonucleolysis of RNA polymerase II transcripts.Nature communications · 2025Article
- Chromatin Transcription Elongation - A Structural Perspective.Journal of molecular biology · 2025Review
- NusG-Spt5 Transcription Factors: Universal, Dynamic Modulators of Gene Expression.Journal of molecular biology · 2025Review
- DNA Gene's Basic Structure as a Nonperturbative Circuit Quantum Electrodynamics: Is RNA Polymerase II the Quantum Bus of Transcription?Current issues in molecular biology · 2024Article
- Structural basis of archaeal RNA polymerase transcription elongation and Spt4/5 recruitment.Nucleic acids research · 2024Article
- Concerted transformation of a hyper-paused transcription complex and its reinforcing protein.Nature communications · 2024Article
- Lowering mutant huntingtin by small molecules relieves Huntington's disease symptoms and progression.EMBO molecular medicine · 2024Article
- Structural and functional basis of the universal transcription factor NusG pro-pausing activity in Mycobacterium tuberculosis.Molecular cell · 2023Article
- The Role ofCells · 2022Article
- DSIF modulates RNA polymerase II occupancy according to template G + C content.NAR genomics and bioinformatics · 2022Article
- Chemical interference with DSIF complex formation lowers synthesis of mutant huntingtin gene products and curtails mutant phenotypes.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Partners in crime: Proteins implicated in RNA repeat expansion diseases.Wiley interdisciplinary reviews. RNA · 2022Review
- Spt5 histone binding activity preserves chromatin during transcription by RNA polymerase II.The EMBO journal · 2022Article
- Metamorphic proteins under a computational microscope: Lessons from a fold-switching RfaH protein.Computational and structural biotechnology journal · 2022Review
- Rho-dependent transcription termination: a revisionist view.Transcription · 2021Review
- Co-Transcriptional RNA Processing in Plants: Exploring from the Perspective of Polyadenylation.International journal of molecular sciences · 2021Review
- Regulation of Eukaryotic RNAPs Activities by Phosphorylation.Frontiers in molecular biosciences · 2021Review
- Coupling of Transcription and Translation in Archaea: Cues From the Bacterial World.Frontiers in microbiology · 2021Article
- Dynamics of the RNA polymerase I TFIIF/TFIIE-like subcomplex: a mini-review.Biochemical Society transactions · 2020Review
- Article
92 more citing papers are in PubMed but not listed here.
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4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
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.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.