ArticleMolecular and cellular biology2002
Redundant cooperative interactions for assembly of a human U6 transcription initiation complex.
Article in Molecular and cellular biology, 2002. 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, 39 citations in OpenAlex.
- Structural insights into distinct mechanisms of RNA polymerase II and III recruitment to snRNA promoters.Nature communications · 2025Article
- Structural basis of human SNAPc recognizing proximal sequence element of snRNA promoter.Nature communications · 2022Article
- Functional and evolutionary analysis of the Arabidopsis 4R-MYB protein SNAPc4 as part of the SNAP complex.Plant physiology · 2021Article
- Article
- Assembly of SNAPc, Bdp1, and TBP on the U6 snRNA Gene Promoter in Drosophila melanogaster.Molecular and cellular biology · 2020Article
- Mechanism of selective recruitment of RNA polymerases II and III to snRNA gene promoters.Genes & development · 2018Article
- Cytoskeletal Filamin A Differentially Modulates RNA Polymerase III Gene Transcription in Transformed Cell Lines.The Journal of biological chemistry · 2016Article
- The Myb domain of the largest subunit of SNAPc adopts different architectural configurations on U1 and U6 snRNA gene promoter sequences.Nucleic acids research · 2014Article
- Identification and characterization of buffalo 7SK and U6 pol III promoters and application for expression of short hairpin RNAs.International journal of molecular sciences · 2014Article
- Architectural arrangement of the small nuclear RNA (snRNA)-activating protein complex 190 subunit (SNAP190) on U1 snRNA gene promoter DNA.The Journal of biological chemistry · 2012Article
- TBP-related factors: a paradigm of diversity in transcription initiation.Cell & bioscience · 2011Article
- Identification of SNAPc subunit domains that interact with specific nucleotide positions in the U1 and U6 gene promoters.Molecular and cellular biology · 2010Article
- A map of Drosophila melanogaster small nuclear RNA-activating protein complex (DmSNAPc) domains involved in subunit assembly and DNA binding.The Journal of biological chemistry · 2009Article
- Co-expression of multiple subunits enables recombinant SNAPC assembly and function for transcription by human RNA polymerases II and III.Protein expression and purification · 2006Article
- Structure-function analysis of the human TFIIB-related factor II protein reveals an essential role for the C-terminal domain in RNA polymerase III transcription.Molecular and cellular biology · 2005Article
- Characterisation and application of a bovine U6 promoter for expression of short hairpin RNAs.BMC biotechnology · 2005Article
- Architectural arrangement of cloned proximal sequence element-binding protein subunits on Drosophila U1 and U6 snRNA gene promoters.Molecular and cellular biology · 2004Article
- Role of the inhibitory DNA-binding surface of human TATA-binding protein in recruitment of human TFIIB family members.Molecular and cellular biology · 2003Article
- Multiple, dispersed human U6 small nuclear RNA genes with varied transcriptional efficiencies.Nucleic acids research · 2003Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The core human U6 promoter consists of a proximal sequence element (PSE) located upstream of a TATA box. The PSE is recognized by the snRNA-activating protein complex (SNAP(c)), which consists of five types of subunits, SNAP190, SNAP50, SNAP45, SNAP43, and SNAP19. The TATA box is recognized by TATA box binding protein (TBP). In addition, basal U6 transcription requires the SANT domain protein Bdp1 and the transcription factor IIB-related factor Brf2. SNAP(c) and mini-SNAP(c), which consists of just SNAP43, SNAP50, and the N-terminal third of SNAP190, bind cooperatively with TBP to the core U6 promoter. By generating complexes smaller than mini-SNAP(c), we have identified a 50-amino-acid region within SNAP190 that is (i) required for cooperative binding with TBP in the context of mini-SNAP(c) and (ii) sufficient for cooperative binding with TBP when fused to a heterologous DNA binding domain. We show that derivatives of mini-SNAP(c) lacking this region are active for transcription and that with such complexes, TBP can still be recruited to the U6 promoter through cooperative interactions with Brf2. Our results identify complexes smaller than mini-SNAP(c) that are transcriptionally active and show that there are at least two redundant mechanisms to stably recruit TBP to the U6 transcription initiation complex.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.