Publications
2000
Adamkewicz J I, Mueller C G, Hansen K E, Prud'homme W A, Thorner J
Purification and enzymic properties of Mot1 ATPase, a regulator of basal transcription in the yeast Saccharomyces cerevisiae Article de journal
Dans: The Journal of Biological Chemistry, vol. 275, no. 28, p. 21158–21168, 2000, ISSN: 0021-9258.
Résumé | Liens | BibTeX | Étiquettes: Adenosine Triphosphatases, Base Sequence, Chromatography, DNA Helicases, DNA-Binding Proteins, Fungal, Gel, Gene Expression Regulation, Genetic, Kinetics, Molecular Sequence Data, Molecular Weight, Osmolar Concentration, Recombinant Proteins, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, TATA Box, TATA-Binding Protein Associated Factors, TATA-Box Binding Protein, Team-Mueller, Transcription, Transcription Factors
@article{adamkewicz_purification_2000,
title = {Purification and enzymic properties of Mot1 ATPase, a regulator of basal transcription in the yeast Saccharomyces cerevisiae},
author = {J I Adamkewicz and C G Mueller and K E Hansen and W A Prud'homme and J Thorner},
doi = {10.1074/jbc.M002639200},
issn = {0021-9258},
year = {2000},
date = {2000-07-01},
journal = {The Journal of Biological Chemistry},
volume = {275},
number = {28},
pages = {21158--21168},
abstract = {The 1867-residue Mot1 protein is a member of a superfamily of ATPases, some of which are helicases, that interact with protein-nucleic acid assemblies. Mot1 is an essential regulator of RNA polymerase II-dependent transcription in vivo and dissociates TATA box-binding protein (TBP)-DNA complexes in vitro. Mot1-(His)(6) was purified to apparent homogeneity from yeast extracts. The preparation efficiently dissociated TBP.TATA complexes, suggesting that no other protein or cofactor is required. Mot1 behaved as a non-globular monomer in hydrodynamic studies, and no association was detected between differentially tagged co-expressed Mot1 constructs. ATPase activity was stimulated about 10-fold by high ionic strength or alkaline pH, or by deletion of the N-terminal TBP-binding segment, suggesting that the N-terminal domain negatively regulates the C-terminal ATPase domain (Mot1C). Correspondingly, at moderate salt concentration, Mot1 ATPase (but not Mot1C) was stimulated textgreater/=10-fold by yeast TBP, suggesting that interaction with TBP relieves a conformational constraint in Mot1. Double- or single-stranded TATA-containing DNA did not affect ATPase activity of Mot1 or Mot1C, with or without TBP. Mot1 did not exhibit detectable helicase activity in strand displacement assays using substrates with flush ends or 5'- or 3'-overhangs. Mot1-catalyzed dissociation of TBP from DNA was not prevented by a psoralen cross-link positioned immediately preceding the TATA sequence. Thus, Mot1 most likely promotes release of TBP from TATA-containing DNA by causing a structural change in TBP itself, rather than by strand unwinding.},
keywords = {Adenosine Triphosphatases, Base Sequence, Chromatography, DNA Helicases, DNA-Binding Proteins, Fungal, Gel, Gene Expression Regulation, Genetic, Kinetics, Molecular Sequence Data, Molecular Weight, Osmolar Concentration, Recombinant Proteins, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, TATA Box, TATA-Binding Protein Associated Factors, TATA-Box Binding Protein, Team-Mueller, Transcription, Transcription Factors},
pubstate = {published},
tppubtype = {article}
}
1994
Auble D T, Hansen K E, Mueller C G, Lane W S, Thorner J, Hahn S
Mot1, a global repressor of RNA polymerase II transcription, inhibits TBP binding to DNA by an ATP-dependent mechanism Article de journal
Dans: Genes & Development, vol. 8, no. 16, p. 1920–1934, 1994, ISSN: 0890-9369.
Résumé | Liens | BibTeX | Étiquettes: Adenosine Triphosphatases, Adenosine Triphosphate, Amino Acid Sequence, Base Sequence, Biological, DNA, DNA Helicases, DNA Probes, DNA-Binding Proteins, Fungal, Fungal Proteins, Genes, Genetic, Models, Molecular Sequence Data, Mutagenesis, Repressor Proteins, RNA Polymerase II, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Site-Directed, TATA Box, TATA-Binding Protein Associated Factors, TATA-Box Binding Protein, Team-Mueller, Transcription, Transcription Factors
@article{auble_mot1_1994,
title = {Mot1, a global repressor of RNA polymerase II transcription, inhibits TBP binding to DNA by an ATP-dependent mechanism},
author = {D T Auble and K E Hansen and C G Mueller and W S Lane and J Thorner and S Hahn},
doi = {10.1101/gad.8.16.1920},
issn = {0890-9369},
year = {1994},
date = {1994-08-01},
journal = {Genes & Development},
volume = {8},
number = {16},
pages = {1920--1934},
abstract = {Basal transcription of many genes in yeast is repressed by Mot1, an essential protein which is a member of the Snf2/Swi2 family of conserved nuclear factors. ADI is an ATP-dependent inhibitor of TATA-binding protein (TBP) binding to DNA that inhibits transcription in vitro. Here we demonstrate that ADI is encoded by the MOT1 gene. Mutation of MOT1 abolishes ADI activity and derepresses basal transcription in vitro and in vivo. Recombinant Mot1 removes TBP from DNA and Mot1 contains an ATPase activity which is essential for its function. Genetic interactions between Mot1 and TBP indicate that their functions are interlinked in vivo. These results provide a general model for understanding the mechanism of action of a large family of nuclear factors involved in processes such as transcription and DNA repair.},
keywords = {Adenosine Triphosphatases, Adenosine Triphosphate, Amino Acid Sequence, Base Sequence, Biological, DNA, DNA Helicases, DNA Probes, DNA-Binding Proteins, Fungal, Fungal Proteins, Genes, Genetic, Models, Molecular Sequence Data, Mutagenesis, Repressor Proteins, RNA Polymerase II, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Site-Directed, TATA Box, TATA-Binding Protein Associated Factors, TATA-Box Binding Protein, Team-Mueller, Transcription, Transcription Factors},
pubstate = {published},
tppubtype = {article}
}