ArticleThe EMBO journal2006
Snf2/Swi2-related ATPase Mot1 drives displacement of TATA-binding protein by gripping DNA.
Article in The EMBO journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
35 citing papers in PubMed, 38 citations in OpenAlex.
- The novel transcriptional activator Bhr1 combining NTPase and Zn(II)2Cys6 DNA-binding domains controls (hemi-)cellulase response to mannose-rich substrates in the white-rot fungusMicrobiology spectrum · 2026Article
- Structural basis for TBP displacement from TATA box DNA by the Swi2/Snf2 ATPase Mot1.Nature structural & molecular biology · 2023Article
- RAD gene family analysis in cotton provides some key genes for flowering and stress tolerance in upland cotton G. hirsutum.BMC genomics · 2022Article
- Structure and mechanism of the RNA polymerase II transcription machinery.Genes & development · 2020Review
- CryoEM structures of Arabidopsis DDR complexes involved in RNA-directed DNA methylation.Nature communications · 2019Article
- Conformational changes and catalytic inefficiency associated with Mot1-mediated TBP-DNA dissociation.Nucleic acids research · 2019Article
- Article
- Molecular Mechanism of Mot1, a TATA-binding Protein (TBP)-DNA Dissociating Enzyme.The Journal of biological chemistry · 2016Article
- Article
- Unraveling the mechanistic features of RNA polymerase II termination by the 5'-3' exoribonuclease Rat1.Nucleic acids research · 2015Article
- Mot1 redistributes TBP from TATA-containing to TATA-less promoters.Molecular and cellular biology · 2013Article
- ATR phosphorylates SMARCAL1 to prevent replication fork collapse.Genes & development · 2013Article
- Swi2/Snf2 remodelers: hybrid views on hybrid molecular machines.Current opinion in structural biology · 2012Review
- 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
- Tight cooperation between Mot1p and NC2β in regulating genome-wide transcription, repression of transcription following heat shock induction and genetic interaction with SAGA.Nucleic acids research · 2012Article
- One small step for Mot1; one giant leap for other Swi2/Snf2 enzymes?Biochimica et biophysica acta · 2011Review
- Coordinated protein and DNA remodeling by human HLTF on stalled replication fork.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- 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
- The RSC chromatin remodelling ATPase translocates DNA with high force and small step size.The EMBO journal · 2011Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Mot1 is a conserved Snf2/Swi2-related transcriptional regulator that uses ATP hydrolysis to displace TATA-binding protein (TBP) from DNA. Several models of the enzymatic mechanism have been proposed, including Mot1-catalyzed distortion of TBP structure, competition between Mot1 and DNA for the TBP DNA-binding surface, and ATP-driven translocation of Mot1 along DNA. Here, DNase I footprinting studies provide strong support for a 'DNA-based' mechanism of Mot1, which we propose involves ATP-driven DNA translocation. Mot1 forms an asymmetric complex with the TBP core domain (TBPc)-DNA complex, contacting DNA both upstream and within the major groove of the TATA Box. Contact with upstream DNA is required for Mot1-mediated displacement of TBPc from DNA. Using the SsoRad54-DNA complex as a model, DNA-binding residues in Mot1 were identified that are critical for Mot1-TBPc-DNA complex formation and catalytic activity, thus placing Mot1 mechanistically within the helicase superfamily. We also report a novel ATP-independent TBPc displacement activity for Mot1 and describe conformational heterogeneity in the Mot1 ATPase, which is likely a general feature of other enzymes in this class.
Indexed as
Identifiers
What OpenQuestion holds
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.