ArticleNucleic acids research2005
The highly conserved glutamic acid 791 of Rpb2 is involved in the binding of NTP and Mg(B) in the active center of human RNA polymerase II.
Article in Nucleic acids research, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 14 citations in OpenAlex.
- Machine learning-based metabolism-related genes signature and immune infiltration landscape in diabetic nephropathy.Frontiers in endocrinology · 2022Article
- Screening for potential nuclear substrates for the plant cell death suppressor kinase Adi3 using peptide microarrays.PloS one · 2020Article
- Molecular dynamics and mutational analysis of the catalytic and translocation cycle of RNA polymerase.BMC biophysics · 2012Article
- Crucial role of a dicarboxylic motif in the catalytic center of yeast RNA polymerases.Current genetics · 2011Article
- Interaction of RNA polymerase II fork loop 2 with downstream non-template DNA regulates transcription elongation.The Journal of biological chemistry · 2011Article
- The RPB2 flap loop of human RNA polymerase II is dispensable for transcription initiation and elongation.Molecular and cellular biology · 2011Article
- Non-canonical DNA transcription enzymes and the conservation of two-barrel RNA polymerases.Nucleic acids research · 2010Review
- Site-directed mutagenesis, purification and assay of Saccharomyces cerevisiae RNA polymerase II.Protein expression and purification · 2010Article
- Transcription elongation by RNA polymerase I is linked to efficient rRNA processing and ribosome assembly.Molecular cell · 2007Article
- Structural perspective on mutations affecting the function of multisubunit RNA polymerases.Microbiology and molecular biology reviews : MMBR · 2006Review
- Functional dissection of the catalytic mechanism of mammalian RNA polymerase II.Biochemistry and cell biology = Biochimie et biologie cellulaire · 2005Review
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
During transcription by RNA polymerase (RNAP) II, the incoming ribonucleoside triphosphate (NTP) enters the catalytic center in association with an Mg2+ ion, termed metal B [Mg(B)]. When bound to RNAP II, Mg(B) is coordinated by the beta and gamma phosphates of the NTP, Rpb1 residues D481 and D483 and Rpb2 residue D837. Rpb2 residue D837 is highly conserved across species. Notably, its neighboring residue, E836 (E791 in human RNAP II), is also highly conserved. To probe the role of E791 in transcription, we have affinity purified and characterized a human RNAP II mutant in which this residue was substituted for alanine. Our results indicate that the transcription activity of the Rpb2 E791A mutant is impaired at low NTP concentrations both in vitro and in vivo. They also revealed that both its NTP polymerization and transcript cleavage activities are decreased at low Mg concentrations. Because Rpb2 residue E791 appears to be located too far from the NTP-Mg(B) complex to make direct contact at either the entry (E) or addition (A) site, we propose alternative mechanisms by which this highly conserved residue participates in loading NTP-Mg(B) in the active site during transcription.
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