ArticleNucleic acids research2005
Crystal structure and RNA binding of the Rpb4/Rpb7 subunits 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 37 papers.
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Who cites it
37 citing papers in PubMed, 72 citations in OpenAlex.
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- Deletion of Elongator Protein 1 (Elp1) relieves heterochromatin defects in a Pol II mutant of Schizosaccharomyces pombe.Genetics · 2026Article
- CTDP1 and RPB7 stabilize Pol II and permit reinitiation.Nature communications · 2025Article
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- Including Protons in Solid-State NMR Resonance Assignment and Secondary Structure Analysis: The Example of RNA Polymerase II Subunits Rpo4/7.Frontiers in molecular biosciences · 2019Article
- Mechanistic Dissection of RNA-Binding Proteins in Regulated Gene Expression at Chromatin Levels.Cold Spring Harbor symposia on quantitative biology · 2019Article
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- Structure of a transcribing RNA polymerase II-DSIF complex reveals a multidentate DNA-RNA clamp.Nature structural & molecular biology · 2017Article
- Factor-dependent archaeal transcription termination.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
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- The HECT domain ubiquitin ligase HUWE1 targets unassembled soluble proteins for degradation.Cell discovery · 2016Article
- The non-coding B2 RNA binds to the DNA cleft and active-site region of RNA polymerase II.Journal of molecular biology · 2013Article
- Uncoupling of mRNA synthesis and degradation impairs adaptation to host temperature in Cryptococcus neoformans.Molecular microbiology · 2013Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
The Rpb4 and Rpb7 subunits of eukaryotic RNA polymerase II (RNAP(II)) form a heterodimer that protrudes from the 10-subunit core of the enzyme. We have obtained crystals of the human Rpb4/Rpb7 heterodimer and determined the structure to 2.7 A resolution. The presence of putative RNA-binding domains on the Rpb7 subunit and the position of the heterodimer close to the RNA exit groove in the 12 subunit yeast polymerase complex strongly suggests a role for the heterodimer in binding and stabilizing the nascent RNA transcript. We have complemented the structural analysis with biochemical studies directed at dissecting the RNA-binding properties of the human Rpb4/Rpb7 complex and that of the homologous E/F complex from Methanocaldococcus jannaschii. A number of conserved, solvent-exposed residues in both the human Rpb7 subunit and the archaeal E subunit have been modified by site-directed mutagenesis and the mutants tested for RNA binding by performing electrophoretic mobility shift assays. These studies have identified an elongated surface region on the corresponding face of both subunit E and Rpb7 that is involved in RNA binding. The area spans the nucleic acid binding face of the OB fold, including the B4-B5 loop, but also extends towards the N-terminal domain.
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