PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
27226635-1	2016	Modifier of transcription 1 (Mot1) is a conserved and essential Swi2/Snf2 ATPase that can remove TATA-binding protein (TBP) from DNA using ATP hydrolysis and in so doing exerts global effects on transcription.	Adenosine Triphosphate	74-77	DNA-binding ATPase	Saccharomyces cerevisiae S288C	0-27
27255709-2	2016	In vitro, Mot1 forms a ternary complex with TBP and DNA and can use ATP hydrolysis to dissociate the TBP-DNA complex.	Adenosine Triphosphate	68-71	DNA-binding ATPase	Saccharomyces cerevisiae S288C	10-14
27255709-8	2016	Moreover, we present biochemical evidence for two distinct conformations of the Mot1 ATPase, the detection of which can be modulated by ATP analogs as well as DNA sequence flanking the TATA sequence.	Adenosine Triphosphate	85-88	DNA-binding ATPase	Saccharomyces cerevisiae S288C	80-84
27226635-1	2016	Modifier of transcription 1 (Mot1) is a conserved and essential Swi2/Snf2 ATPase that can remove TATA-binding protein (TBP) from DNA using ATP hydrolysis and in so doing exerts global effects on transcription.	Adenosine Triphosphate	74-77	DNA-binding ATPase	Saccharomyces cerevisiae S288C	29-33
23851461-3	2013	We find that yeast TAF1-TAND1, which in itself acts as a transcriptional activator, binds TBP"s concave DNA-binding surface by presenting similar anchor residues to TBP as does Mot1 but from a distinct structural scaffold.	tributyl phosphate	90-93	DNA-binding ATPase	Saccharomyces cerevisiae S288C	177-181
23851461-4	2013	Furthermore, we show how TAF1-TAND2 uses an aromatic and acidic anchoring pattern to bind a conserved TBP surface groove traversing the basic helix region, and we find highly similar TBP-binding motifs also presented by the structurally distinct TFIIA, Mot1 and Brf1 proteins.	tributyl phosphate	183-186	DNA-binding ATPase	Saccharomyces cerevisiae S288C	253-257
18703679-7	2008	ATP hydrolysis releases NC2 and DNA from the Mot1p-TBP complex.	Adenosine Triphosphate	0-3	DNA-binding ATPase	Saccharomyces cerevisiae S288C	45-50
21444714-9	2011	The data suggest that Mot1 uses ATP hydrolysis to redistribute accessible TBP away from intrinsically preferred sites to other sites of intrinsically low preference.	Adenosine Triphosphate	32-35	DNA-binding ATPase	Saccharomyces cerevisiae S288C	22-26
21075799-3	2011	Here, using a formaldehyde-based in vivo cross-linking and chromatin immunoprecipitation assay in conjunction with transcriptional, mutational and co-immunoprecipitational analyses, we show that CBC is recruited to the body of yeast gene, and then stimulates the formation of pre-initiation complex (PIC) at several yeast promoters through its interaction with Mot1p (modifier of transcription).	Formaldehyde	14-26	DNA-binding ATPase	Saccharomyces cerevisiae S288C	361-366
19139279-4	2009	Here, we demonstrate that Mot1 is SUMOylated in vivo and that disrupting the Slx5-Slx8 pathway by mutation of the target lysines in Mot1, by deletion of SLX5 or the ubiquitin E2 UBC4, or by inhibition of the proteosome suppresses mot1-301 mutant phenotypes and increases the stability of the Mot1-301 protein.	Lysine	121-128	DNA-binding ATPase	Saccharomyces cerevisiae S288C	26-30
19139279-4	2009	Here, we demonstrate that Mot1 is SUMOylated in vivo and that disrupting the Slx5-Slx8 pathway by mutation of the target lysines in Mot1, by deletion of SLX5 or the ubiquitin E2 UBC4, or by inhibition of the proteosome suppresses mot1-301 mutant phenotypes and increases the stability of the Mot1-301 protein.	Lysine	121-128	DNA-binding ATPase	Saccharomyces cerevisiae S288C	132-136
19139279-4	2009	Here, we demonstrate that Mot1 is SUMOylated in vivo and that disrupting the Slx5-Slx8 pathway by mutation of the target lysines in Mot1, by deletion of SLX5 or the ubiquitin E2 UBC4, or by inhibition of the proteosome suppresses mot1-301 mutant phenotypes and increases the stability of the Mot1-301 protein.	Lysine	121-128	DNA-binding ATPase	Saccharomyces cerevisiae S288C	132-136
19139279-6	2009	In support of this idea, growth of Saccharomyces cerevisiae in the presence of the arginine analog canavanine results in increased SUMOylation and Slx5-Slx8-mediated degradation of wild-type Mot1.	Arginine	83-91	DNA-binding ATPase	Saccharomyces cerevisiae S288C	191-195
19139279-6	2009	In support of this idea, growth of Saccharomyces cerevisiae in the presence of the arginine analog canavanine results in increased SUMOylation and Slx5-Slx8-mediated degradation of wild-type Mot1.	Canavanine	99-109	DNA-binding ATPase	Saccharomyces cerevisiae S288C	191-195
19098311-2	2009	Biochemical and structural results support a model in which ATP binding and hydrolysis induce a conformational change in Mot1 that drives local translocation along DNA, thus removing TBP.	Adenosine Triphosphate	60-63	DNA-binding ATPase	Saccharomyces cerevisiae S288C	121-125
18606810-2	2008	Mot1 uses ATP hydrolysis to displace TBP from DNA, an activity that can be readily reconciled with its global role in gene repression.	Adenosine Triphosphate	10-13	DNA-binding ATPase	Saccharomyces cerevisiae S288C	0-4
18077439-5	2007	An antisense RNA strategy over the MoT1 gene showed that interference of the expression of this gene leads to the inhibition of molybdate transport activity and, in turn, of the Mo-containing enzyme nitrate reductase, indicating a function of MoT1 in molybdate transport.	molybdate	128-137	DNA-binding ATPase	Saccharomyces cerevisiae S288C	35-39
18077439-5	2007	An antisense RNA strategy over the MoT1 gene showed that interference of the expression of this gene leads to the inhibition of molybdate transport activity and, in turn, of the Mo-containing enzyme nitrate reductase, indicating a function of MoT1 in molybdate transport.	molybdate	128-137	DNA-binding ATPase	Saccharomyces cerevisiae S288C	243-247
18077439-5	2007	An antisense RNA strategy over the MoT1 gene showed that interference of the expression of this gene leads to the inhibition of molybdate transport activity and, in turn, of the Mo-containing enzyme nitrate reductase, indicating a function of MoT1 in molybdate transport.	molybdate	251-260	DNA-binding ATPase	Saccharomyces cerevisiae S288C	35-39
18077439-5	2007	An antisense RNA strategy over the MoT1 gene showed that interference of the expression of this gene leads to the inhibition of molybdate transport activity and, in turn, of the Mo-containing enzyme nitrate reductase, indicating a function of MoT1 in molybdate transport.	molybdate	251-260	DNA-binding ATPase	Saccharomyces cerevisiae S288C	243-247
18077439-7	2007	Molybdate uptake mediated by MOT1 showed a K(m) of approximately 6 nM, which is the range of the lowest K(m) values reported and was activated in the presence of nitrate.	molybdate	0-9	DNA-binding ATPase	Saccharomyces cerevisiae S288C	29-33
18077439-7	2007	Molybdate uptake mediated by MOT1 showed a K(m) of approximately 6 nM, which is the range of the lowest K(m) values reported and was activated in the presence of nitrate.	Nitrates	162-169	DNA-binding ATPase	Saccharomyces cerevisiae S288C	29-33
16415371-5	2006	Among the genes we cloned is MOT1, encoding a repressor that inhibits TBP binding to the promoter, thus linking glucose repression with TBP access to chromatin.	Glucose	112-119	DNA-binding ATPase	Saccharomyces cerevisiae S288C	29-33
18003916-4	2007	MOT1 is required for efficient uptake and translocation of molybdate and for normal growth under conditions of limited molybdate supply.	molybdate	59-68	DNA-binding ATPase	Saccharomyces cerevisiae S288C	0-4
18003916-4	2007	MOT1 is required for efficient uptake and translocation of molybdate and for normal growth under conditions of limited molybdate supply.	molybdate	119-128	DNA-binding ATPase	Saccharomyces cerevisiae S288C	0-4
18003916-5	2007	Kinetics studies in yeast revealed that the K(m) value of MOT1 for molybdate is approximately 20 nM.	molybdate	67-76	DNA-binding ATPase	Saccharomyces cerevisiae S288C	58-62
12805227-1	2003	Yeast Mot1p, an abundant conserved member of the Snf2p-ATPase family of proteins, both dissociates TBP from DNA in vitro using the energy of ATP and represses gene transcription in vivo, yet paradoxically, loss of Mot1p function also leads to decreased transcription of certain genes.	tributyl phosphate	99-102	DNA-binding ATPase	Saccharomyces cerevisiae S288C	6-11
12805227-1	2003	Yeast Mot1p, an abundant conserved member of the Snf2p-ATPase family of proteins, both dissociates TBP from DNA in vitro using the energy of ATP and represses gene transcription in vivo, yet paradoxically, loss of Mot1p function also leads to decreased transcription of certain genes.	Adenosine Triphosphate	55-58	DNA-binding ATPase	Saccharomyces cerevisiae S288C	6-11
12571241-0	2003	Mot1 regulates the DNA binding activity of free TATA-binding protein in an ATP-dependent manner.	Adenosine Triphosphate	75-78	DNA-binding ATPase	Saccharomyces cerevisiae S288C	0-4
12571241-1	2003	Mot1 is an essential Snf2/Swi2-related Saccharomyces cerevisiae protein that binds the TATA-binding protein (TBP) and removes TBP from DNA using ATP hydrolysis.	Adenosine Triphosphate	145-148	DNA-binding ATPase	Saccharomyces cerevisiae S288C	0-4
12571241-8	2003	Residues on the DNA-binding surface of TBP are important for Mot1 binding and the Mot1.TBP binary complex binds very poorly to DNA and does not dissociate in the presence of ATP.	Adenosine Triphosphate	174-177	DNA-binding ATPase	Saccharomyces cerevisiae S288C	82-86
12571241-10	2003	A model for Mot1 action is proposed in which ATP hydrolysis causes the Mot1 N terminus to displace the TATA box, leading to ejection of Mot1 and TBP from DNA.	Adenosine Triphosphate	45-48	DNA-binding ATPase	Saccharomyces cerevisiae S288C	12-16
12571241-10	2003	A model for Mot1 action is proposed in which ATP hydrolysis causes the Mot1 N terminus to displace the TATA box, leading to ejection of Mot1 and TBP from DNA.	Adenosine Triphosphate	45-48	DNA-binding ATPase	Saccharomyces cerevisiae S288C	71-75
12571241-10	2003	A model for Mot1 action is proposed in which ATP hydrolysis causes the Mot1 N terminus to displace the TATA box, leading to ejection of Mot1 and TBP from DNA.	Adenosine Triphosphate	45-48	DNA-binding ATPase	Saccharomyces cerevisiae S288C	71-75
12417716-1	2002	Mot1 stably associates with the TATA-binding protein (TBP), and it can dissociate TBP from DNA in an ATP-dependent manner.	Adenosine Triphosphate	101-104	DNA-binding ATPase	Saccharomyces cerevisiae S288C	0-4
11880621-2	2002	In vitro, Mot1 can disrupt TATA-binding protein-DNA complexes in an ATP-dependent reaction.	Adenosine Triphosphate	68-71	DNA-binding ATPase	Saccharomyces cerevisiae S288C	10-14
11880621-6	2002	These findings suggest a novel function for the Mot1 ATPase at activated genes, perhaps involving ATP-driven reorganization of the preinitiation complex.	Adenosine Triphosphate	53-56	DNA-binding ATPase	Saccharomyces cerevisiae S288C	48-52
11296235-2	2001	Here we examine the mechanism of action of MOT1, a yeast SNF2/SWI2-related ATPase that uses ATP hydrolysis to remove TATA binding protein (TBP) from DNA.	Adenosine Triphosphate	75-78	DNA-binding ATPase	Saccharomyces cerevisiae S288C	43-47
11296235-7	2001	Combining these results with proposed similarities between SNF2/SWI2 ATPases and helicases, we suggest that MOT1 uses ATP hydrolysis to translocate along the handle and thereby disrupt interactions between TBP and DNA.	Adenosine Triphosphate	69-72	DNA-binding ATPase	Saccharomyces cerevisiae S288C	108-112
10887203-7	2000	Correspondingly, at moderate salt concentration, Mot1 ATPase (but not Mot1C) was stimulated >/=10-fold by yeast TBP, suggesting that interaction with TBP relieves a conformational constraint in Mot1.	Salts	29-33	DNA-binding ATPase	Saccharomyces cerevisiae S288C	49-53
10760173-3	2000	Mot1p is an ATPase that removes DNA-bound TBP upon ATP hydrolysis.	tributyl phosphate	42-45	DNA-binding ATPase	Saccharomyces cerevisiae S288C	0-5
10760173-3	2000	Mot1p is an ATPase that removes DNA-bound TBP upon ATP hydrolysis.	Adenosine Triphosphate	12-15	DNA-binding ATPase	Saccharomyces cerevisiae S288C	0-5
10082549-1	1999	MOT1 is an ATPase which can dissociate TATA binding protein (TBP)-DNA complexes in a reaction requiring ATP hydrolysis.	Adenosine Triphosphate	11-14	DNA-binding ATPase	Saccharomyces cerevisiae S288C	0-4
9234740-0	1997	Molecular analysis of the SNF2/SWI2 protein family member MOT1, an ATP-driven enzyme that dissociates TATA-binding protein from DNA.	Adenosine Triphosphate	67-70	DNA-binding ATPase	Saccharomyces cerevisiae S288C	58-62
9858565-5	1999	MOT1 is an essential Saccharomyces cerevisiae transcription factor that uses ATP to dissociate TATA binding protein (TBP) from DNA.	Adenosine Triphosphate	77-80	DNA-binding ATPase	Saccharomyces cerevisiae S288C	0-4
9858565-7	1999	The results demonstrate that, following ATP-dependent TBP-DNA dissociation, MOT1 dissociates rapidly from the DNA by a mechanism that does not require a DNA end.	Adenosine Triphosphate	40-43	DNA-binding ATPase	Saccharomyces cerevisiae S288C	76-80
9858565-8	1999	Template commitment footprinting experiments support the conclusion that ATP-dependent DNA tracking by MOT1 does not occur.	Adenosine Triphosphate	73-76	DNA-binding ATPase	Saccharomyces cerevisiae S288C	103-107
9858565-9	1999	These results support a model in which MOT1 drives TBP-DNA dissociation by a mechanism that involves a transient, ATP-dependent interaction with TBP-DNA which does not involve ATP-dependent DNA tracking.	Adenosine Triphosphate	114-117	DNA-binding ATPase	Saccharomyces cerevisiae S288C	39-43
9488487-8	1998	Together, these findings suggest that human TAF-172 is the functional homolog of yeast Mot1 and uses the energy of ATP hydrolysis to remove TBP (but apparently not TBP-TAF complexes) from DNA.	Adenosine Triphosphate	115-118	DNA-binding ATPase	Saccharomyces cerevisiae S288C	87-91
9234740-5	1997	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.	Adenosine Triphosphate	25-28	DNA-binding ATPase	Saccharomyces cerevisiae S288C	35-39
9234740-5	1997	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.	Adenosine Triphosphate	111-114	DNA-binding ATPase	Saccharomyces cerevisiae S288C	35-39
9234740-6	1997	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.	Adenosine Triphosphate	95-98	DNA-binding ATPase	Saccharomyces cerevisiae S288C	90-94
9234740-8	1997	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.	Adenosine Triphosphate	131-134	DNA-binding ATPase	Saccharomyces cerevisiae S288C	6-10
9234740-8	1997	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.	Adenosine Triphosphate	131-134	DNA-binding ATPase	Saccharomyces cerevisiae S288C	126-130
9121454-1	1997	BUR3 and BUR6 were identified previously by selecting for mutations that increase transcription from an upstream activating sequence (UAS)-less promoter in Saccharomyces cerevisiae.	Phenindione	134-137	DNA-binding ATPase	Saccharomyces cerevisiae S288C	0-4
9121454-4	1997	BUR3 is identical to MOT1, a previously characterized essential gene that encodes an ATP-dependent inhibitor of the TATA box-binding protein.	Adenosine Triphosphate	85-88	DNA-binding ATPase	Saccharomyces cerevisiae S288C	0-4
9121454-4	1997	BUR3 is identical to MOT1, a previously characterized essential gene that encodes an ATP-dependent inhibitor of the TATA box-binding protein.	Adenosine Triphosphate	85-88	DNA-binding ATPase	Saccharomyces cerevisiae S288C	21-25
8972209-4	1997	In this way, we have identified a mutation in MOT1, which encodes an ATP-dependent inhibitor of TBP binding to TATA boxes: Previous analyses suggested that Mot1 causes repression in vivo.	Adenosine Triphosphate	69-72	DNA-binding ATPase	Saccharomyces cerevisiae S288C	46-50
8972209-4	1997	In this way, we have identified a mutation in MOT1, which encodes an ATP-dependent inhibitor of TBP binding to TATA boxes: Previous analyses suggested that Mot1 causes repression in vivo.	Adenosine Triphosphate	69-72	DNA-binding ATPase	Saccharomyces cerevisiae S288C	156-160
7958867-0	1994	Mot1, a global repressor of RNA polymerase II transcription, inhibits TBP binding to DNA by an ATP-dependent mechanism.	Adenosine Triphosphate	95-98	DNA-binding ATPase	Saccharomyces cerevisiae S288C	0-4
8293972-4	1993	In addition to some previously studied genes, this selection has identified five genes that we have designated BUR1, BUR2, BUR3, BUR5 and BUR6 (for Bypass UAS Requirement).	Phenindione	155-158	DNA-binding ATPase	Saccharomyces cerevisiae S288C	123-127