ArticleMolecular and cellular biology1996
Rpo26p, a subunit common to yeast RNA polymerases, is essential for the assembly of RNA polymerases I and II and for the stability of the largest subunits of these enzymes.
Article in Molecular and cellular biology, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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18 citing papers in PubMed, 42 citations in OpenAlex.
- Molecular Evolution of the Archaeal DNA-Dependent RNA Polymerase: Cooperative Changes in Subunit Composition and Specific Domains of Small Subunits.International journal of molecular sciences · 2026Article
- Widespread epistasis shapes RNA polymerase II active site function and evolution.Nature communications · 2025Article
- RNA Pol II Assembly Affects ncRNA Expression.International journal of molecular sciences · 2023Article
- Structures of transcription preinitiation complex engaged with the +1 nucleosome.Nature structural & molecular biology · 2023Article
- Three human RNA polymerases interact with TFIIH via a common RPB6 subunit.Nucleic acids research · 2022Article
- Several Isoforms for Each Subunit Shared by RNA Polymerases are Differentially Expressed in the Cultivated Olive Tree (Frontiers in molecular biosciences · 2021Article
- Biogenesis of RNA Polymerases in Yeast.Frontiers in molecular biosciences · 2021Review
- The ω Subunit Governs RNA Polymerase Stability and Transcriptional Specificity in Staphylococcus aureus.Journal of bacteriology · 2017Article
- Small things considered: the small accessory subunits of RNA polymerase in Gram-positive bacteria.FEMS microbiology reviews · 2015Review
- Two Routes to Genetic Suppression of RNA Trimethylguanosine Cap Deficiency via C-Terminal Truncation of U1 snRNP Subunit Snp1 or Overexpression of RNA Polymerase Subunit Rpo26.G3 (Bethesda, Md.) · 2015Article
- 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
- Site specific phosphorylation of yeast RNA polymerase I.Nucleic acids research · 2008Article
- 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
- Partners of Rpb8p, a small subunit shared by yeast RNA polymerases I, II and III.Molecular and cellular biology · 2001Article
- Bacterial RNA polymerase subunit omega and eukaryotic RNA polymerase subunit RPB6 are sequence, structural, and functional homologs and promote RNA polymerase assembly.Proceedings of the National Academy of Sciences of the United States of America · 2001Article
- The Rpb6 subunit of fission yeast RNA polymerase II is a contact target of the transcription elongation factor TFIIS.Molecular and cellular biology · 2000Article
- Genetic evidence for selective degradation of RNA polymerase subunits by the 20S proteasome in Saccharomyces cerevisiae.Nucleic acids research · 1997Article
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3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Eukaryotic nuclear RNA polymerases (RNAPs) are composed of two large subunits and a number of small polypeptides, some of which are common among these enzymes. To understand the function of Rpo26p, one of the five subunits common to yeast RNAPs, 34 different mutations have been isolated in RP026 that cause cell death in a strain carrying a temperature-sensitive (ts) mutation in the gene (RP021) encoding the largest subunit of RNAPII. These mutant alleles were grouped into three phenotypic classes (null, ts, and neutral) on the basis of the phenotype they imposed in combination with wild-type RP021. The function of Rpo26p was addressed by biochemical analysis of the ts rpo26-31 allele. The steady-state level of rpo26-31p was reduced at high temperature; this was accompanied by a decrease in the level of at least two other subunits, the largest subunits of RNAPI (A190p) and RNAPII (Rpo21p). Pulse-chase metabolic labeling and immunoprecipitation of RNAPII showed that at high temperature, rpo26-31 did not lead to dissociation of Rpo26p from the polymerase but prevented the assembly of RNAPII. Overexpression of rpo26-31 partially suppressed the ts phenotype and led to accumulation of the mutant subunit. However, overexpression only marginally suppressed the assembly defect of RNAPII. Furthermore, A190p and Rpo21p continued to accumulate at low levels under these conditions. We suggest that Rpo26p is essential for the assembly of RNAPI and RNAPII and for the stability of the largest subunits of these enzymes.
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