ArticleMolecular and cellular biology2018
Functions of the TFIIE-Related Tandem Winged-Helix Domain of Rpc34 in RNA Polymerase III Initiation and Elongation.
Article in Molecular and cellular biology, 2018. 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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Who cites it
10 citing papers in PubMed.
- Dynamic positioning of Rpc34 winged helix in RNA polymerase III elongation complex for its stability with implications for reinitiation.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Mutational and biophysical analyses reveal a TFIIIC binding region in the TFIIF-related Rpc53 subunit of RNA polymerase III.The Journal of biological chemistry · 2023Article
- Proteotoxicity caused by perturbed protein complexes underlies hybrid incompatibility in yeast.Nature communications · 2022Article
- Knockdown NRPC2, 3, 8, NRPABC1 and NRPABC2 Affects RNAPIII Activity and Disrupts Seed Development in Arabidopsis.International journal of molecular sciences · 2021Article
- Structure of human RNA polymerase III elongation complex.Cell research · 2021Article
- Dynamics of the RNA polymerase I TFIIF/TFIIE-like subcomplex: a mini-review.Biochemical Society transactions · 2020Review
- A mutation in POLR3E impairs antiviral immune response and RNA polymerase III.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Conditional depletion of the RNA polymerase I subunit PAF53 reveals that it is essential for mitosis and enables identification of functional domains.The Journal of biological chemistry · 2019Article
- RNA polymerase III subunits C37/53 modulate rU:dA hybrid 3' end dynamics during transcription termination.Nucleic acids research · 2019Article
- Structural visualization of RNA polymerase III transcription machineries.Cell discovery · 2018Article
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2 authors.
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Abstract
Rpc34 is a subunit of the Rpc82/34/31 subcomplex residing on the DNA-binding cleft of RNA polymerase (Pol) III. Rpc34 contains a structurally flexible N-terminal tandem winged-helix (tWH) domain related to the TFIIE transcription factor. While the second WH (WH2) fold of the tWH domain is known to function in DNA melting activity during transcription initiation, the functional role of the WH1 fold is unknown. In this study, we generated a series of new Rpc34 tWH mutants conferring a cold-sensitive growth phenotype. We found that the tWH mutations severely compromised
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