ArticleThe Journal of biological chemistry2008
Function and structural organization of Mot1 bound to a natural target promoter.
Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 17 citations in OpenAlex.
- Structural basis for TBP displacement from TATA box DNA by the Swi2/Snf2 ATPase Mot1.Nature structural & molecular biology · 2023Article
- Article
- Conformational changes and catalytic inefficiency associated with Mot1-mediated TBP-DNA dissociation.Nucleic acids research · 2019Article
- Molecular Mechanism of Mot1, a TATA-binding Protein (TBP)-DNA Dissociating Enzyme.The Journal of biological chemistry · 2016Article
- Mot1 redistributes TBP from TATA-containing to TATA-less promoters.Molecular and cellular biology · 2013Article
- Measuring chromatin interaction dynamics on the second time scale at single-copy genes.Science (New York, N.Y.) · 2013Article
- One small step for Mot1; one giant leap for other Swi2/Snf2 enzymes?Biochimica et biophysica acta · 2011Review
- Genome-wide transcriptional dependence on conserved regions of Mot1.Molecular and cellular biology · 2011Article
- The basal initiation machinery: beyond the general transcription factors.Current opinion in cell biology · 2009Review
- TATA-binding protein variants that bypass the requirement for Mot1 in vivo.The Journal of biological chemistry · 2009Article
- The dynamic personality of TATA-binding protein.Trends in biochemical sciences · 2009Article
- Imaging transcription in living cells.Annual review of biophysics · 2009Review
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Mot1 is an essential, conserved TATA-binding protein (TBP)-associated factor in Saccharomyces cerevisiae and a member of the Snf2/Swi2 ATPase family. Mot1 uses ATP hydrolysis to displace TBP from DNA, an activity that can be readily reconciled with its global role in gene repression. Less well understood is how Mot1 directly activates gene expression. It has been suggested that Mot1-mediated activation can occur by displacement of inactive TBP-containing complexes from promoters, thereby permitting assembly of functional transcription complexes. Mot1 may also activate transcription by other mechanisms that have not yet been defined. A gap in our understanding has been the absence of biochemical information related to the activity of Mot1 on natural target genes. Using URA1 as a model Mot1-activated promoter, we show striking differences in the way that both TBP and Mot1 interact with DNA compared with other model DNA substrates analyzed previously. These differences are due at least in part to the propensity of TBP alone to bind to the URA1 promoter in the wrong orientation to direct appropriate assembly of the URA1 preinitiation complex. The results suggest that Mot1-mediated activation of URA1 transcription involves at least two steps, one of which is the removal of TBP bound to the promoter in the opposite orientation required for URA1 transcription.
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Registered trials
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.