ArticleProceedings of the National Academy of Sciences of the United States of America2000
Crystal structure of RPB5, a universal eukaryotic RNA polymerase subunit and transcription factor interaction target.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 38 citations in OpenAlex.
- Novel B cell epitopes mapping in pD205R protein of African swine fever virus using monoclonal antibodies.BMC veterinary research · 2026Article
- The Order-Disorder Continuum: Linking Predictions of Protein Structure and Disorder through Molecular Simulation.Scientific reports · 2020Review
- 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
- Article
- Sequence, structure and functional diversity of PD-(D/E)XK phosphodiesterase superfamily.Nucleic acids research · 2012Article
- Crystallization and preliminary X-ray analysis of the RPB5 subunit of human RNA polymerase II.Acta crystallographica. Section F, Structural biology and crystallization communications · 2011Article
- RPB5-mediating protein is required for the proliferation of hepatocellular carcinoma cells.The Journal of biological chemistry · 2011Article
- Article
- Evolution of complex RNA polymerases: the complete archaeal RNA polymerase structure.PLoS biology · 2009Article
- PolV(PolIVb) function in RNA-directed DNA methylation requires the conserved active site and an additional plant-specific subunit.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- Diversification of function by different isoforms of conventionally shared RNA polymerase subunits.Molecular biology of the cell · 2007Article
- Functional organization of the Rpb5 subunit shared by the three yeast RNA polymerases.Nucleic acids research · 2007Article
- An inactivated nuclease-like domain in RecC with novel function: implications for evolution.BMC structural biology · 2005Article
- Identification of a new family of putative PD-(D/E)XK nucleases with unusual phylogenomic distribution and a new type of the active site.BMC genomics · 2005Article
- Inference of relationships in the 'twilight zone' of homology using a combination of bioinformatics and site-directed mutagenesis: a case study of restriction endonucleases Bsp6I and PvuII.Nucleic acids research · 2005Article
- Archaeal RNA polymerase subunits F and P are bona fide homologs of eukaryotic RPB4 and RPB12.Nucleic acids research · 2000Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Eukaryotic nuclei contain three different types of RNA polymerases (RNAPs), each consisting of 12-18 different subunits. The evolutionarily highly conserved RNAP subunit RPB5 is shared by all three enzymes and therefore represents a key structural/functional component of all eukaryotic RNAPs. Here we present the crystal structure of the RPB5 subunit from Saccharomyces cerevisiae. The bipartite structure includes a eukaryote-specific N-terminal domain and a C-terminal domain resembling the archaeal RNAP subunit H. RPB5 has been implicated in direct protein-protein contacts with transcription factor IIB, one of the components of the RNAP(II) basal transcriptional machinery, and gene-specific activator proteins, such as the hepatitis B virus transactivator protein X. The experimentally mapped regions of RPB5 involved in these interactions correspond to distinct and surface-exposed alpha-helical structures.
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