ArticleJournal of bacteriology1998
Rpb4, a subunit of RNA polymerase II, enables the enzyme to transcribe at temperature extremes in vitro.
Article in Journal of bacteriology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed.
- Functional State of Lampbrush Chromosomes in Early Vitellogenic Oocytes of Hibernating FrogsJournal of developmental biology · 2026Article
- Article
- Rpb9-deficient cells are defective in DNA damage response and require histone H3 acetylation for survival.Scientific reports · 2018Article
- Article
- Rpb4 subunit functions mainly in mRNA synthesis by RNA polymerase II.The Journal of biological chemistry · 2014Article
- Cotranscriptional assembly of mRNP complexes that determine the cytoplasmic fate of mRNA.Transcription · 2011Article
- Structure of the 12-subunit RNA polymerase II refined with the aid of anomalous diffraction data.The Journal of biological chemistry · 2009Article
- Transcription in the nucleus and mRNA decay in the cytoplasm are coupled processes.Genes & development · 2008Article
- Rtr1 is the Saccharomyces cerevisiae homolog of a novel family of RNA polymerase II-binding proteins.Eukaryotic cell · 2008Article
- Genomic location of the human RNA polymerase II general machinery: evidence for a role of TFIIF and Rpb7 at both early and late stages of transcription.The Biochemical journal · 2008Article
- The Rpb7p subunit of yeast RNA polymerase II plays roles in the two major cytoplasmic mRNA decay mechanisms.The Journal of cell biology · 2007Article
- Basal transcription machinery: role in regulation of stress response in eukaryotes.Journal of biosciences · 2007Review
- Nucleocytoplasmic shuttling of the Rpb4p and Rpb7p subunits of Saccharomyces cerevisiae RNA polymerase II by two pathways.Eukaryotic cell · 2006Article
- The RNA polymerase II subunit Rpb4p mediates decay of a specific class of mRNAs.Genes & development · 2005Article
- "Sleeping beauty": quiescence in Saccharomyces cerevisiae.Microbiology and molecular biology reviews : MMBR · 2004Review
- Domainal organization of the lower eukaryotic homologs of the yeast RNA polymerase II core subunit Rpb7 reflects functional conservation.Nucleic acids research · 2004Article
- Identification of the RNA polymerase II subunit hsRPB7 as a novel target of the von Hippel-Lindau protein.The EMBO journal · 2003Article
- Structural and functional homology between the RNAP(I) subunits A14/A43 and the archaeal RNAP subunits E/F.Nucleic acids research · 2003Article
- Rpb4p, a subunit of RNA polymerase II, mediates mRNA export during stress.Molecular biology of the cell · 2003Article
- Two different Drosophila ADA2 homologues are present in distinct GCN5 histone acetyltransferase-containing complexes.Molecular and cellular biology · 2003Article
Corrections and comments
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2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Rpb4 is a subunit of Saccharomyces cerevisiae RNA polymerase II (Pol II). It associates with the polymerase preferentially in stationary phase and is essential for some stress responses. Using the promoter-independent initiation and chain elongation assay, we monitored Pol II enzymatic activity in cell extracts. We show here that Rpb4 is required for the polymerase activity at temperature extremes (10 and 35 degreesC). In contrast, at moderate temperature (23 degreesC) Pol II activity is independent of Rpb4. These results are consistent with the role previously attributed to Rpb4 as a subunit whose association with Pol II helps Pol II to transcribe during extreme temperatures. The enzymatic inactivation of Pol II lacking Rpb4 at the nonoptimal temperature was prevented by the addition of recombinant Rpb4 produced in Escherichia coli prior to the in vitro reaction assay. This finding suggests that modification of Rpb4 is not required for its functional association with the other Pol II subunits. Sucrose gradient and immunoprecipitation experiments demonstrated that Rpb4 is present in the cell in excess over the Pol II complex during all growth phases. Nevertheless, the rescue of Pol II activity at the nonoptimal temperature by Rpb4 is possible only when cell extracts are obtained from postlogarithmic cells, not from logarithmically growing cells. This result suggests that Pol II molecules should be modified in order to recruit Rpb4; the portion of the modified Pol II molecules is small during logarithmic phase and becomes predominant in stationary phase.
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