ArticleMolecular and cellular biology2000
The Rpb6 subunit of fission yeast RNA polymerase II is a contact target of the transcription elongation factor TFIIS.
Article in Molecular and cellular biology, 2000. 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, 41 citations in OpenAlex.
- Article
- Never a dull enzyme, RNA polymerase II.Transcription · 2023Review
- Structures of transcription preinitiation complex engaged with the +1 nucleosome.Nature structural & molecular biology · 2023Article
- A remodeled RNA polymerase II complex catalyzing viroid RNA-templated transcription.PLoS pathogens · 2022Article
- Lighting up Nobel Prize-winning studies with protein intrinsic disorder.Cellular and molecular life sciences : CMLS · 2022Review
- Three human RNA polymerases interact with TFIIH via a common RPB6 subunit.Nucleic acids research · 2022Article
- Quantitative analysis of asynchronous transcription-translation and transcription processivity iniScience · 2021Article
- Gene expression profiling of epidermal cell types in C. elegans using Targeted DamID.Development (Cambridge, England) · 2021Article
- Distinct pathways of RNA polymerase regulation by a phage-encoded factor.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Characterization of the RNA polymerase II and III complexes in Leishmania major.International journal for parasitology · 2007Article
- Mutations in the RNA polymerase III subunit Rpc11p that decrease RNA 3' cleavage activity increase 3'-terminal oligo(U) length and La-dependent tRNA processing.Molecular and cellular biology · 2005Article
- Functional interaction between TFIIB and the Rpb2 subunit of RNA polymerase II: implications for the mechanism of transcription initiation.Molecular and cellular biology · 2004Article
- RNA polymerase II transcription apparatus in Schizosaccharomyces pombe.Current genetics · 2004Review
- Loss of the Rpb4/Rpb7 subcomplex in a mutant form of the Rpb6 subunit shared by RNA polymerases I, II, and III.Molecular and cellular biology · 2003Article
- von Hippel-Lindau protein binds hyperphosphorylated large subunit of RNA polymerase II through a proline hydroxylation motif and targets it for ubiquitination.Proceedings of the National Academy of Sciences of the United States of America · 2003Article
- Subnuclear localization and Cajal body targeting of transcription elongation factor TFIIS in amphibian oocytes.Molecular biology of the cell · 2003Article
- Use of RNA yeast polymerase II mutants in studying transcription elongation.Methods in enzymology · 2003Article
- RNA polymerase II complexes in the very early phase of transcription are not susceptible to TFIIS-induced exonucleolytic cleavage.Nucleic acids research · 2002Article
- Regulation of an IMP dehydrogenase gene and its overexpression in drug-sensitive transcription elongation mutants of yeast.The Journal of biological chemistry · 2001Article
- Analysis of the open region of RNA polymerase II transcription complexes in the early phase of elongation.Nucleic acids research · 2001Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Rpb6 subunit of RNA polymerase II is one of the five subunits common to three forms of eukaryotic RNA polymerase. Deletion and truncation analyses of the rpb6 gene in the fission yeast Schizosaccharomyces pombe indicated that Rpb6, consisting of 142 amino acid residues, is an essential protein for cell viability, and the essential region is located in the C-terminal half between residues 61 and 139. After random mutagenesis, a total of 14 temperature-sensitive mutants were isolated, each carrying a single (or double in three cases and triple in one) mutation. Four mutants each carrying a single mutation in the essential region were sensitive to 6-azauracil (6AU), which inhibits transcription elongation by depleting the intracellular pool of GTP and UTP. Both 6AU sensitivity and temperature-sensitive phenotypes of these rpb6 mutants were suppressed by overexpression of TFIIS, a transcription elongation factor. In agreement with the genetic studies, the mutant RNA polymerases containing the mutant Rpb6 subunits showed reduced affinity for TFIIS, as measured by a pull-down assay of TFIIS-RNA polymerase II complexes using a fusion form of TFIIS with glutathione S-transferase. Moreover, the direct interaction between TFIIS and RNA polymerase II was competed by the addition of Rpb6. Taken together, the results lead us to propose that Rpb6 plays a role in the interaction between RNA polymerase II and the transcription elongation factor TFIIS.
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