ArticleMolecular and cellular biology2001
A novel upstream RNA polymerase III promoter element becomes essential when the chromatin structure of the yeast U6 RNA gene is altered.
Article in Molecular and cellular biology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 33 citations in OpenAlex.
- Yeast U6 snRNA made by RNA polymerase II is less stable but functional.RNA (New York, N.Y.) · 2022Article
- Structural Features of the Nucleosomal DNA Modulate the Functional Binding of a Transcription Factor and Productive Transcription.Frontiers in genetics · 2022Article
- The HMGB chromatin protein Nhp6A can bypass obstacles when traveling on DNA.Nucleic acids research · 2020Article
- The life of U6 small nuclear RNA, from cradle to grave.RNA (New York, N.Y.) · 2018Review
- A novel downstream regulatory element cooperates with the silencing machinery to repress EPA1 expression in Candida glabrata.Genetics · 2012Article
- In vivo analysis of Caenorhabditis elegans noncoding RNA promoter motifs.BMC molecular biology · 2008Article
- Requirement of Nhp6 proteins for transcription of a subset of tRNA genes and heterochromatin barrier function in Saccharomyces cerevisiae.Molecular and cellular biology · 2007Article
- Article
- Reconfiguring the connectivity of a multiprotein complex: fusions of yeast TATA-binding protein with Brf1, and the function of transcription factor IIIB.Proceedings of the National Academy of Sciences of the United States of America · 2005Article
- Modulation of differential transcription of tRNA genes through chromatin organization.The Biochemical journal · 2005Article
- Role for Nhp6, Gcn5, and the Swi/Snf complex in stimulating formation of the TATA-binding protein-TFIIA-DNA complex.Molecular and cellular biology · 2004Article
- TATA-binding protein mutants that are lethal in the absence of the Nhp6 high-mobility-group protein.Molecular and cellular biology · 2004Article
- High-level activation of transcription of the yeast U6 snRNA gene in chromatin by the basal RNA polymerase III transcription factor TFIIIC.Molecular and cellular biology · 2004Article
- Nhp6 facilitates Aft1 binding and Ssn6 recruitment, both essential for FRE2 transcriptional activation.The EMBO journal · 2004Article
- Position-dependent function of a B block promoter element implies a specialized chromatin structure on the S.cerevisiae U6 RNA gene, SNR6.Nucleic acids research · 2004Article
- Regulation of TATA-binding protein binding by the SAGA complex and the Nhp6 high-mobility group protein.Molecular and cellular biology · 2003Article
- A single-stranded promoter for RNA polymerase III.Proceedings of the National Academy of Sciences of the United States of America · 2003Article
- Regulation of pol III transcription by nutrient and stress signaling pathways.Biochimica et biophysica actaReview
- Nhp6: a small but powerful effector of chromatin structure in Saccharomyces cerevisiae.Biochimica et biophysica actaReview
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The Saccharomyces cerevisiae U6 RNA gene, SNR6, possesses upstream sequences that allow productive binding in vitro of the RNA polymerase III (Pol III) transcription initiation factor IIIB (TFIIIB) in the absence of TFIIIC or other assembly factors. TFIIIC-independent transcription of SNR6 in vitro is highly sensitive to point mutations in a consensus TATA box at position -30. In contrast, the TATA box is dispensable for SNR6 transcription in vivo, apparently because TFIIIC bound to the intragenic A block and downstream B block can recruit TFIIIB via protein-protein interactions. A mutant allele of SNR6 with decreased spacing between the A and B blocks, snr6-Delta42, exhibits increased dependence on the upstream sequences in vivo. Unexpectedly, we find that in vivo expression of snr6-Delta42 is much more sensitive to mutations in a (dT-dA)(7) tract between the TATA box and transcription start site than to mutations in the TATA box itself. Inversion of single base pairs in the center of the dT-dA tract nearly abolishes transcription of snr6-Delta42, yet inversion of all 7 base pairs has little effect on expression, indicating that the dA-dT tract is relatively orientation independent. Although it is within the TFIIIB footprint, point mutations in the dT-dA tract do not inhibit TFIIIB binding or TFIIIC-independent transcription of SNR6 in vitro. In the absence of the chromatin architectural protein Nhp6, dT-dA tract mutations are lethal even when A-to-B block spacing is wild type. We conclude that the (dT-dA)(7) tract and Nhp6 cooperate to direct productive transcription complex assembly on SNR6 in vivo.
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