ArticleMolecular and cellular biology1997
Molecular analysis of the SNF2/SWI2 protein family member MOT1, an ATP-driven enzyme that dissociates TATA-binding protein from DNA.
Article in Molecular and cellular biology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.
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Who cites it
52 citing papers in PubMed, 96 citations in OpenAlex.
- The CSB chromatin remodeler regulates PARP1- and PARP2-mediated single-strand break repair at actively transcribed DNA regions.Nucleic acids research · 2023Article
- Structural basis for TBP displacement from TATA box DNA by the Swi2/Snf2 ATPase Mot1.Nature structural & molecular biology · 2023Article
- On the Role of TATA Boxes and TATA-Binding Protein inPlants (Basel, Switzerland) · 2023Review
- Dynamic Interplay between Cockayne Syndrome Protein B and Poly(ADP-Ribose) Polymerase 1 during Oxidative DNA Damage Repair.Biomedicines · 2022Article
- Conformational changes and catalytic inefficiency associated with Mot1-mediated TBP-DNA dissociation.Nucleic acids research · 2019Article
- miR-132 suppresses transcription of ribosomal proteins to promote protective Th1 immunity.EMBO reports · 2019Article
- Article
- DNA residence time is a regulatory factor of transcription repression.Nucleic acids research · 2017Article
- Mot1, Ino80C, and NC2 Function Coordinately to Regulate Pervasive Transcription in Yeast and Mammals.Molecular cell · 2017Article
- An efficient targeted nuclease strategy for high-resolution mapping of DNA binding sites.eLife · 2017Article
- Molecular Mechanism of Mot1, a TATA-binding Protein (TBP)-DNA Dissociating Enzyme.The Journal of biological chemistry · 2016Article
- The Modifier of Transcription 1 (Mot1) ATPase and Spt16 Histone Chaperone Co-regulate Transcription through Preinitiation Complex Assembly and Nucleosome Organization.The Journal of biological chemistry · 2016Article
- Article
- Suppression of intragenic transcription requires the MOT1 and NC2 regulators of TATA-binding protein.Nucleic acids research · 2014Article
- Two-step mechanism for modifier of transcription 1 (Mot1) enzyme-catalyzed displacement of TATA-binding protein (TBP) from DNA.The Journal of biological chemistry · 2012Article
- One small step for Mot1; one giant leap for other Swi2/Snf2 enzymes?Biochimica et biophysica acta · 2011Review
- Structure and mechanism of the Swi2/Snf2 remodeller Mot1 in complex with its substrate TBP.Nature · 2011Article
- Genome-wide transcriptional dependence on conserved regions of Mot1.Molecular and cellular biology · 2011Article
- Proteomics reveals a physical and functional link between hepatocyte nuclear factor 4alpha and transcription factor IID.The Journal of biological chemistry · 2009Article
- Transcription dynamics.Molecular cell · 2009Review
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
MOT1 is an essential Saccharomyces cerevisiae protein and a member of the SNF2/SWI2 family of ATPases. MOT1 functions by removing TATA-binding protein (TBP) from DNA, and as a consequence, MOT1 can regulate transcription both in vitro and in vivo. Here we describe the in vivo and in vitro activities of MOT1 deletion and substitution mutants. The results indicate that MOT1 is targeted to TBP both in vitro and in vivo via amino acids in its nonconserved N terminus. The conserved C-terminal ATPase of MOT1 appears to contribute to TBP-DNA complex recognition in the absence of ATP, but it appears to function primarily during the actual ATP-dependent dissociation reaction. Chimeric proteins in which homologous portions of SNF2/SWI2 have been substituted for the MOT1 ATPase can bind to TBP-DNA complexes but fail to dissociate these complexes in the presence of ATP, suggesting that the specificity of action of MOT1 is also conferred by the C-terminal ATPase. ATPase assays demonstrate that the MOT1 ATPase is activated by TBP. Thus, MOT1 undergoes at least two conformational changes: (i) an allosteric effect of TBP that mediates the activation of the MOT1 ATPase and (ii) an ATP-driven "power stroke" that causes TBP-DNA complex dissociation. These results provide a general framework for understanding how members of the SNF2/SWI2 protein family use ATP to modulate protein-DNA interactions to regulate many diverse processes in cells.
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