ArticleNucleic acids research2007
Functional organization of the Rpb5 subunit shared by the three yeast RNA polymerases.
Article in Nucleic acids research, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed.
- The H3K27me3 reader UAD-2 recruits a TAF-12-containing transcription machinery to initiate piRNA expression within heterochromatic clusters.Nature communications · 2025Article
- Never a dull enzyme, RNA polymerase II.Transcription · 2023Review
- A remodeled RNA polymerase II complex catalyzing viroid RNA-templated transcription.PLoS pathogens · 2022Article
- Several Isoforms for Each Subunit Shared by RNA Polymerases are Differentially Expressed in the Cultivated Olive Tree (Frontiers in molecular biosciences · 2021Article
- Regulation of Eukaryotic RNAPs Activities by Phosphorylation.Frontiers in molecular biosciences · 2021Review
- Prefoldin-like Bud27 influences the transcription of ribosomal components and ribosome biogenesis inRNA (New York, N.Y.) · 2020Article
- Rpb5, a subunit shared by eukaryotic RNA polymerases, cooperates with prefoldin-like Bud27/URI.AIMS genetics · 2018Review
- Cloning, soluble expression, and purification of the RNA polymerase II subunit RPB5 from Saccharomyces cerevisiae.Bioengineered · 2015Article
- The yeast prefoldin-like URI-orthologue Bud27 associates with the RSC nucleosome remodeler and modulates transcription.Nucleic acids research · 2014Article
- Article
- Correct assembly of RNA polymerase II depends on the foot domain and is required for multiple steps of transcription in Saccharomyces cerevisiae.Molecular and cellular biology · 2013Article
- RMP plays distinct roles in the proliferation of hepatocellular carcinoma cells and normal hepatic cells.International journal of biological sciences · 2013Article
- The prefoldin bud27 mediates the assembly of the eukaryotic RNA polymerases in an rpb5-dependent manner.PLoS genetics · 2013Article
- Sequence, structure and functional diversity of PD-(D/E)XK phosphodiesterase superfamily.Nucleic acids research · 2012Article
- The conserved foot domain of RNA pol II associates with proteins involved in transcriptional initiation and/or early elongation.Genetics · 2011Article
- RNA polymerase II conserved protein domains as platforms for protein-protein interactions.Transcription · 2011Article
- RPB5-mediating protein is required for the proliferation of hepatocellular carcinoma cells.The Journal of biological chemistry · 2011Article
- Non-canonical DNA transcription enzymes and the conservation of two-barrel RNA polymerases.Nucleic acids research · 2010Review
- Integrative structure modeling of macromolecular assemblies from proteomics data.Molecular & cellular proteomics : MCP · 2010Article
- Rearrangement of the RNA polymerase subunit H and the lower jaw in archaeal elongation complexes.Nucleic acids research · 2010Article
Corrections and comments
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Rpb5, a subunit shared by the three yeast RNA polymerases, combines a eukaryotic N-terminal module with a globular C-end conserved in all non-bacterial enzymes. Conditional and lethal mutants of the moderately conserved eukaryotic module showed that its large N-terminal helix and a short motif at the end of the module are critical in vivo. Lethal or conditional mutants of the C-terminal globe altered the binding of Rpb5 to Rpb1-beta25/26 (prolonging the Bridge helix) and Rpb1-alpha44/47 (ahead of the Switch 1 loop and binding Rpb5 in a two-hybrid assay). The large intervening segment of Rpb1 is held across the DNA Cleft by Rpb9, consistent with the synergy observed for rpb5 mutants and rpb9Delta or its RNA polymerase I rpa12Delta counterpart. Rpb1-beta25/26, Rpb1-alpha44/45 and the Switch 1 loop were only found in Rpb5-containing polymerases, but the Bridge and Rpb1-alpha46/47 helix bundle were universally conserved. We conclude that the main function of the dual Rpb5-Rpb1 binding and the Rpb9-Rpb1 interaction is to hold the Bridge helix, the Rpb1-alpha44/47 helix bundle and the Switch 1 loop into a closely packed DNA-binding fold around the transcription bubble, in an organization shared by the two other nuclear RNA polymerases and by the archaeal and viral enzymes.
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