ArticleNucleic acids research2003
Structural and functional homology between the RNAP(I) subunits A14/A43 and the archaeal RNAP subunits E/F.
Article in Nucleic acids research, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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10 citing papers in PubMed, 27 citations in OpenAlex.
- Crystal structure of the Bloom's syndrome helicase indicates a role for the HRDC domain in conformational changes.Nucleic acids research · 2015Article
- Review
- Crystal structure of the C17/25 subcomplex from Schizosaccharomyces pombe RNA polymerase III.Protein science : a publication of the Protein Society · 2011Article
- Transcription in the nucleus and mRNA decay in the cytoplasm are coupled processes.Genes & development · 2008Article
- Crystallization of RNA polymerase I subcomplex A14/A43 by iterative prediction, probing and removal of flexible regions.Acta crystallographica. Section F, Structural biology and crystallization communications · 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
- Active RNA polymerase I of Trypanosoma brucei harbors a novel subunit essential for transcription.Molecular and cellular biology · 2007Article
- RNA polymerase I-specific subunit CAST/hPAF49 has a role in the activation of transcription by upstream binding factor.Molecular and cellular biology · 2006Article
- The RNA polymerase I transcription machinery.Biochemical Society symposium · 2006Review
- Crystal structure and RNA binding of the Rpb4/Rpb7 subunits of human RNA polymerase II.Nucleic acids research · 2005Article
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Authors and funding
6 authors at 1 institution in 1 country.
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Abstract
In the archaeal RNA polymerase and the eukaryotic RNA polymerase II, two subunits (E/F and RPB4/RPB7, respectively) form a heterodimer that reversibly associates with the core of the enzyme. Recently it has emerged that this heterodimer also has a counterpart in the other eukaryotic RNA polymerases: in particular two subunits of RNA polymerase I (A14 and A43) display genetic and biochemical characteristics that are similar to those of the RPB4 and RPB7 subunits, despite the fact that only A43 shows some sequence homology to RPB7. We demonstrate that the sequence of A14 strongly suggests the presence of a HRDC domain, a motif that is found at the C-terminus of a number of helicases and RNases. The same motif is also seen in the structure of the F subunit, suggesting a structural link between A14 and the RPB4/C17/subunit F family, even in the absence of direct sequence homology. We show that it is possible to co-express and co-purify large amounts of the recombinant A14/A43 heterodimer, indicating a tight and specific interaction between the two subunits. To shed light on the function of the heterodimer, we performed gel mobility shift assays and showed that the A14/A43 heterodimer binds single-stranded RNA in a similar way to the archaeal E/F complex.
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