Single-molecule states link transcription factor binding to gene expression

The binding of multiple transcription factors (TFs) to genomic enhancers drives gene expression in mammalian cells 1 . However, the molecular details that link enhancer sequence to TF binding, promoter state and transcription levels remain unclear. Here we applied single-molecule footprinting 2 , 3...

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Published in:	Nature (London) Vol. 636; no. 8043; pp. 745 - 754
Main Authors:	Doughty, Benjamin R., Hinks, Michaela M., Schaepe, Julia M., Marinov, Georgi K., Thurm, Abby R., Rios-Martinez, Carolina, Parks, Benjamin E., Tan, Yingxuan, Marklund, Emil, Dubocanin, Danilo, Bintu, Lacramioara, Greenleaf, William J.
Format:	Journal Article
Language:	English
Published:	London Nature Publishing Group UK 19.12.2024 Nature Publishing Group
Subjects:	13 13/106 38 45/15 45/23 45/91 631/208/200 631/337/100 631/337/572 631/553/552 Binding Sites Chromatin DNA - genetics DNA - metabolism DNA Footprinting DNA Methylation Enhancer Elements, Genetic Enhancers Gene expression Gene Expression Regulation Humanities and Social Sciences Humans Interferon Type I - metabolism K562 Cells Kinetics Mammalian cells Models, Molecular multidisciplinary Nucleosomes Nucleosomes - genetics Nucleosomes - metabolism Nucleotide sequence Promoter Regions, Genetic Protein Binding Proteins Regulatory proteins Regulatory sequences Response Elements RNA polymerase Science Science (multidisciplinary) Single Molecule Imaging Statistical mechanics Thermodynamics Transcription factors Transcription Factors - metabolism
ISSN:	0028-0836, 1476-4687, 1476-4687
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Abstract	The binding of multiple transcription factors (TFs) to genomic enhancers drives gene expression in mammalian cells 1 . However, the molecular details that link enhancer sequence to TF binding, promoter state and transcription levels remain unclear. Here we applied single-molecule footprinting 2 , 3 to measure the simultaneous occupancy of TFs, nucleosomes and other regulatory proteins on engineered enhancer–promoter constructs with variable numbers of TF binding sites for both a synthetic TF and an endogenous TF involved in the type I interferon response. Although TF binding events on nucleosome-free DNA are independent, activation domains recruit cofactors that destabilize nucleosomes, driving observed TF binding cooperativity. Average TF occupancy linearly determines promoter activity, and we decompose TF strength into separable binding and activation terms. Finally, we develop thermodynamic and kinetic models that quantitatively predict both the enhancer binding microstates and gene expression dynamics. This work provides a template for the quantitative dissection of distinct contributors to gene expression, including TF activation domains, concentration, binding affinity, binding site configuration and recruitment of chromatin regulators. A study uses single-molecule footprinting to measure protein occupancy at regulatory elements on individual molecules in human cells and describes how different properties of transcription factor binding contribute to gene expression.
AbstractList	The binding of multiple transcription factors (TFs) to genomic enhancers drives gene expression in mammalian cells. However, the molecular details that link enhancer sequence to TF binding, promoter state and transcription levels remain unclear. Here we applied single-molecule footprinting to measure the simultaneous occupancy of TFs, nucleosomes and other regulatory proteins on engineered enhancer–promoter constructs with variable numbers of TF binding sites for both a synthetic TF and an endogenous TF involved in the type I interferon response. Although TF binding events on nucleosome-free DNA are independent, activation domains recruit cofactors that destabilize nucleosomes, driving observed TF binding cooperativity. Average TF occupancy linearly determines promoter activity, and we decompose TF strength into separable binding and activation terms. Finally, we develop thermodynamic and kinetic models that quantitatively predict both the enhancer binding microstates and gene expression dynamics. This work provides a template for the quantitative dissection of distinct contributors to gene expression, including TF activation domains, concentration, binding affinity, binding site configuration and recruitment of chromatin regulators. The binding of multiple transcription factors (TFs) to genomic enhancers drives gene expression in mammalian cells 1 . However, the molecular details that link enhancer sequence to TF binding, promoter state and transcription levels remain unclear. Here we applied single-molecule footprinting 2 , 3 to measure the simultaneous occupancy of TFs, nucleosomes and other regulatory proteins on engineered enhancer–promoter constructs with variable numbers of TF binding sites for both a synthetic TF and an endogenous TF involved in the type I interferon response. Although TF binding events on nucleosome-free DNA are independent, activation domains recruit cofactors that destabilize nucleosomes, driving observed TF binding cooperativity. Average TF occupancy linearly determines promoter activity, and we decompose TF strength into separable binding and activation terms. Finally, we develop thermodynamic and kinetic models that quantitatively predict both the enhancer binding microstates and gene expression dynamics. This work provides a template for the quantitative dissection of distinct contributors to gene expression, including TF activation domains, concentration, binding affinity, binding site configuration and recruitment of chromatin regulators. A study uses single-molecule footprinting to measure protein occupancy at regulatory elements on individual molecules in human cells and describes how different properties of transcription factor binding contribute to gene expression. The binding of multiple transcription factors (TFs) to genomic enhancers drives gene expression in mammalian cells . However, the molecular details that link enhancer sequence to TF binding, promoter state and transcription levels remain unclear. Here we applied single-molecule footprinting to measure the simultaneous occupancy of TFs, nucleosomes and other regulatory proteins on engineered enhancer-promoter constructs with variable numbers of TF binding sites for both a synthetic TF and an endogenous TF involved in the type I interferon response. Although TF binding events on nucleosome-free DNA are independent, activation domains recruit cofactors that destabilize nucleosomes, driving observed TF binding cooperativity. Average TF occupancy linearly determines promoter activity, and we decompose TF strength into separable binding and activation terms. Finally, we develop thermodynamic and kinetic models that quantitatively predict both the enhancer binding microstates and gene expression dynamics. This work provides a template for the quantitative dissection of distinct contributors to gene expression, including TF activation domains, concentration, binding affinity, binding site configuration and recruitment of chromatin regulators. The binding of multiple transcription factors (TFs) to genomic enhancers drives gene expression in mammalian cells'. However, the molecular details that link enhancer sequence to TF binding, promoter state and transcription levels remain unclear. Here we applied single-molecule footprinting2,3 to measure the simultaneous occupancy of TFs, nucleosomes and other regulatory proteins on engineered enhancer-promoter constructs with variable numbers of TF binding sites for both a synthetic TF andan endogenous TF involved in the type l interferon response. Although TF binding events on nucleosome-free DNA are independent, activation domains recruit cofactors that destabilize nucleosomes, driving observed TF binding cooperativity. Average TF occupancy linearly determines promoter activity, and we decompose TF strength into separable binding and activation terms. Finally, we develop thermodynamic and kinetic models that quantitatively predict both the enhancer binding microstates and gene expression dynamics. This work provides a template for the quantitative dissection of distinct contributors to gene expression, including TF activation domains, concentration, binding affinity, binding site configuration and recruitment of chromatin regulators. The binding of multiple transcription factors (TFs) to genomic enhancers drives gene expression in mammalian cells1. However, the molecular details that link enhancer sequence to TF binding, promoter state and transcription levels remain unclear. Here we applied single-molecule footprinting2,3 to measure the simultaneous occupancy of TFs, nucleosomes and other regulatory proteins on engineered enhancer-promoter constructs with variable numbers of TF binding sites for both a synthetic TF and an endogenous TF involved in the type I interferon response. Although TF binding events on nucleosome-free DNA are independent, activation domains recruit cofactors that destabilize nucleosomes, driving observed TF binding cooperativity. Average TF occupancy linearly determines promoter activity, and we decompose TF strength into separable binding and activation terms. Finally, we develop thermodynamic and kinetic models that quantitatively predict both the enhancer binding microstates and gene expression dynamics. This work provides a template for the quantitative dissection of distinct contributors to gene expression, including TF activation domains, concentration, binding affinity, binding site configuration and recruitment of chromatin regulators.The binding of multiple transcription factors (TFs) to genomic enhancers drives gene expression in mammalian cells1. However, the molecular details that link enhancer sequence to TF binding, promoter state and transcription levels remain unclear. Here we applied single-molecule footprinting2,3 to measure the simultaneous occupancy of TFs, nucleosomes and other regulatory proteins on engineered enhancer-promoter constructs with variable numbers of TF binding sites for both a synthetic TF and an endogenous TF involved in the type I interferon response. Although TF binding events on nucleosome-free DNA are independent, activation domains recruit cofactors that destabilize nucleosomes, driving observed TF binding cooperativity. Average TF occupancy linearly determines promoter activity, and we decompose TF strength into separable binding and activation terms. Finally, we develop thermodynamic and kinetic models that quantitatively predict both the enhancer binding microstates and gene expression dynamics. This work provides a template for the quantitative dissection of distinct contributors to gene expression, including TF activation domains, concentration, binding affinity, binding site configuration and recruitment of chromatin regulators.
Author	Doughty, Benjamin R. Marklund, Emil Greenleaf, William J. Schaepe, Julia M. Marinov, Georgi K. Thurm, Abby R. Tan, Yingxuan Parks, Benjamin E. Bintu, Lacramioara Rios-Martinez, Carolina Hinks, Michaela M. Dubocanin, Danilo
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Cites_doi	10.1016/j.molcel.2017.01.007 10.1038/nbt.2486 10.1016/j.cell.2014.05.038 10.1007/978-1-4939-6716-2_2 10.1016/j.gde.2005.02.007 10.1038/30032 10.1101/gr.266551.120 10.1021/acs.jmedchem.8b01318 10.1007/978-1-4939-6716-2_1 10.1016/j.cels.2023.02.003 10.1038/s41586-022-04570-y 10.1073/pnas.89.12.5547 10.1074/jbc.272.7.4600 10.1038/nmeth.4401 10.1038/nmeth.4396 10.1101/2024.06.14.599019 10.1128/MCB.24.10.4476-4486.2004 10.1146/annurev-biochem-040320-103630 10.1126/science.7792603 10.1038/nsmb.1500 10.1128/MCB.22.6.1615-1625.2002 10.1101/2024.05.30.596689 10.1126/science.1198817 10.1016/j.cell.2018.04.033 10.1016/0092-8674(93)90051-Q 10.1016/j.tig.2009.08.003 10.1038/nprot.2012.101 10.1101/gad.7.2.173 10.1002/JLB.2MIR0817-342R 10.1016/j.molcel.2024.01.027 10.1016/j.immuni.2019.03.025 10.1073/pnas.0913805107 10.1016/j.cell.2020.11.024 10.1038/nature24028 10.1016/j.cell.2015.12.032 10.1016/j.molcel.2021.03.008 10.1016/S1097-2765(00)00054-X 10.1101/gad.12.5.599 10.1038/nbt.1754 10.1101/gr.143008.112 10.1073/pnas.1718426115 10.1084/jem.20111680 10.1186/s13072-015-0009-5 10.1016/j.molcel.2017.06.027 10.1038/s41586-020-2528-x 10.1371/journal.pbio.0040309 10.1038/s41592-019-0686-2 10.1016/j.molcel.2021.12.008 10.1038/ng.3646 10.1016/0022-2836(90)90187-Q 10.1101/2023.04.11.536490 10.1016/j.cell.2023.10.006 10.1146/annurev-biophys-121219-081542 10.1038/s41467-019-10970-y 10.1073/pnas.79.4.1129 10.1101/2022.07.22.501078 10.1016/j.cyto.2015.07.019 10.1126/science.aaz1646 10.1186/gb-2009-10-3-r25 10.1101/gad.13.18.2369 10.1073/pnas.1911188117 10.1016/j.molcel.2020.11.015 10.1038/nrg3207 10.1016/0092-8674(91)90354-2 10.1038/s41588-024-01706-w 10.5281/zenodo.13841007 10.1186/s13059-014-0550-8 10.1073/pnas.85.2.382 10.1016/j.jmb.2004.11.056 10.1038/s41586-023-05906-y 10.1038/s41587-022-01494-w 10.7554/eLife.64320 10.1101/gad.4.10.1753 10.1016/j.molcel.2011.06.016 10.1038/nature09692 10.1128/MCB.01180-12 10.1038/s41588-020-00768-w 10.1038/s41592-019-0730-2 10.1016/S1097-2765(00)80216-6 10.1016/0092-8674(95)90136-1 10.5281/zenodo.13840888 10.1016/j.molcel.2023.12.004
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References	K Cui (8219_CR45) 2004; 24 8219_CR83 Z Wunderlich (8219_CR5) 2009; 25 MG Durrant (8219_CR67) 2023; 41 8219_CR82 S Chong (8219_CR35) 2014; 158 S Rengachari (8219_CR42) 2018; 115 SC Biddie (8219_CR10) 2011; 43 R Shelansky (8219_CR60) 2020; 117 E Giniger (8219_CR6) 1988; 85 DY Lee (8219_CR53) 1993; 72 J Tycko (8219_CR68) 2020; 183 J Feng (8219_CR80) 2012; 7 A Rada-Iglesias (8219_CR30) 2011; 470 HM Lazear (8219_CR40) 2019; 50 M Gossen (8219_CR19) 1995; 268 CD Krause (8219_CR47) 2015; 76 8219_CR48 N Yudkovsky (8219_CR24) 1999; 13 A Raj (8219_CR33) 2006; 4 DM Suter (8219_CR34) 2011; 332 S Mostafavi (8219_CR49) 2016; 164 R Vaisvila (8219_CR63) 2024; 84 Z Shipony (8219_CR14) 2020; 17 JT Robinson (8219_CR75) 2011; 29 GK Marinov (8219_CR78) 2017; 1543 8219_CR72 F Wong (8219_CR59) 2020; 49 8219_CR71 TK Kelly (8219_CR2) 2012; 22 K Struhl (8219_CR54) 1998; 12 C Sönmezer (8219_CR16) 2021; 81 M Pettersson (8219_CR7) 1990; 214 H Boeger (8219_CR58) 2022; 91 LA Mirny (8219_CR9) 2010; 107 HA Bluyssen (8219_CR43) 1997; 272 P Virtanen (8219_CR73) 2020; 17 AB Stergachis (8219_CR15) 2020; 368 BT Weinert (8219_CR70) 2018; 174 CJ Fryer (8219_CR11) 1998; 393 J Vierstra (8219_CR4) 2020; 583 M Iurlaro (8219_CR69) 2021; 53 JPN Papillon (8219_CR26) 2018; 61 N Alerasool (8219_CR29) 2022; 82 8219_CR61 TK Kundu (8219_CR28) 2000; 6 N Dogan (8219_CR50) 2015; 8 R Martinez-Corral (8219_CR13) 2023; 14 MC Patel (8219_CR44) 2013; 33 8219_CR65 8219_CR64 8219_CR62 F Spitz (8219_CR1) 2012; 13 T Narita (8219_CR55) 2021; 81 D Herschlag (8219_CR12) 1993; 7 LM Lasko (8219_CR32) 2017; 550 J Zuin (8219_CR37) 2022; 604 B Langmead (8219_CR79) 2009; 10 KE Neely (8219_CR23) 1999; 4 8219_CR27 JY Xiao (8219_CR36) 2021; 10 MR Corces (8219_CR74) 2017; 14 D Thanos (8219_CR8) 1995; 83 MR Corces (8219_CR51) 2016; 48 R Vaisvila (8219_CR20) 2021; 31 RD Kornberg (8219_CR57) 1991; 67 AN Schep (8219_CR76) 2017; 14 MT Weirauch (8219_CR52) 2013; 31 GK Ackers (8219_CR21) 1982; 79 E Platanitis (8219_CR41) 2019; 10 B Brower-Toland (8219_CR31) 2005; 346 M Levo (8219_CR17) 2017; 65 KE Neely (8219_CR25) 2002; 22 L Bintu (8219_CR18) 2005; 15 HD Kim (8219_CR22) 2008; 15 8219_CR56 AR Krebs (8219_CR3) 2017; 67 MI Love (8219_CR77) 2014; 15 J Manry (8219_CR46) 2011; 208 M Gossen (8219_CR38) 1992; 89 N DelRosso (8219_CR66) 2023; 616 DS Kessler (8219_CR39) 1990; 4 GK Marinov (8219_CR81) 2017; 1543 38352517 - bioRxiv. 2024 Feb 04:2024.02.02.578660. doi: 10.1101/2024.02.02.578660.
References_xml	– volume: 65 start-page: 604 year: 2017 ident: 8219_CR17 publication-title: Mol. Cell doi: 10.1016/j.molcel.2017.01.007 – volume: 31 start-page: 126 year: 2013 ident: 8219_CR52 publication-title: Nat. Biotechnol. doi: 10.1038/nbt.2486 – volume: 158 start-page: 314 year: 2014 ident: 8219_CR35 publication-title: Cell doi: 10.1016/j.cell.2014.05.038 – volume: 1543 start-page: 19 year: 2017 ident: 8219_CR81 publication-title: Methods Mol. Biol. doi: 10.1007/978-1-4939-6716-2_2 – volume: 15 start-page: 116 year: 2005 ident: 8219_CR18 publication-title: Curr. Opin. Genet. Dev. doi: 10.1016/j.gde.2005.02.007 – volume: 393 start-page: 88 year: 1998 ident: 8219_CR11 publication-title: Nature doi: 10.1038/30032 – volume: 31 start-page: 1280 year: 2021 ident: 8219_CR20 publication-title: Genome Res. doi: 10.1101/gr.266551.120 – volume: 61 start-page: 10155 year: 2018 ident: 8219_CR26 publication-title: J. Med. Chem. doi: 10.1021/acs.jmedchem.8b01318 – volume: 1543 start-page: 3 year: 2017 ident: 8219_CR78 publication-title: Methods Mol. Biol. doi: 10.1007/978-1-4939-6716-2_1 – volume: 14 start-page: 324 year: 2023 ident: 8219_CR13 publication-title: Cell Syst. doi: 10.1016/j.cels.2023.02.003 – volume: 604 start-page: 571 year: 2022 ident: 8219_CR37 publication-title: Nature doi: 10.1038/s41586-022-04570-y – volume: 89 start-page: 5547 year: 1992 ident: 8219_CR38 publication-title: Proc. Natl Acad. Sci. USA doi: 10.1073/pnas.89.12.5547 – volume: 272 start-page: 4600 year: 1997 ident: 8219_CR43 publication-title: J. Biol. Chem. doi: 10.1074/jbc.272.7.4600 – volume: 14 start-page: 975 year: 2017 ident: 8219_CR76 publication-title: Nat. Methods doi: 10.1038/nmeth.4401 – volume: 14 start-page: 959 year: 2017 ident: 8219_CR74 publication-title: Nat. Methods doi: 10.1038/nmeth.4396 – ident: 8219_CR64 doi: 10.1101/2024.06.14.599019 – volume: 24 start-page: 4476 year: 2004 ident: 8219_CR45 publication-title: Mol. Cell. Biol. doi: 10.1128/MCB.24.10.4476-4486.2004 – volume: 91 start-page: 423 year: 2022 ident: 8219_CR58 publication-title: Annu. Rev. Biochem. doi: 10.1146/annurev-biochem-040320-103630 – volume: 268 start-page: 1766 year: 1995 ident: 8219_CR19 publication-title: Science doi: 10.1126/science.7792603 – volume: 15 start-page: 1192 year: 2008 ident: 8219_CR22 publication-title: Nat. Struct. Mol. Biol. doi: 10.1038/nsmb.1500 – volume: 22 start-page: 1615 year: 2002 ident: 8219_CR25 publication-title: Mol. Cell. Biol. doi: 10.1128/MCB.22.6.1615-1625.2002 – ident: 8219_CR62 doi: 10.1101/2024.05.30.596689 – volume: 332 start-page: 472 year: 2011 ident: 8219_CR34 publication-title: Science doi: 10.1126/science.1198817 – volume: 174 start-page: 231 year: 2018 ident: 8219_CR70 publication-title: Cell doi: 10.1016/j.cell.2018.04.033 – volume: 72 start-page: 73 year: 1993 ident: 8219_CR53 publication-title: Cell doi: 10.1016/0092-8674(93)90051-Q – volume: 25 start-page: 434 year: 2009 ident: 8219_CR5 publication-title: Trends Genet. doi: 10.1016/j.tig.2009.08.003 – volume: 7 start-page: 1728 year: 2012 ident: 8219_CR80 publication-title: Nat. Protoc. doi: 10.1038/nprot.2012.101 – volume: 7 start-page: 173 year: 1993 ident: 8219_CR12 publication-title: Genes Dev. doi: 10.1101/gad.7.2.173 – ident: 8219_CR48 doi: 10.1002/JLB.2MIR0817-342R – volume: 84 start-page: 854 year: 2024 ident: 8219_CR63 publication-title: Mol. Cell doi: 10.1016/j.molcel.2024.01.027 – volume: 50 start-page: 907 year: 2019 ident: 8219_CR40 publication-title: Immunity doi: 10.1016/j.immuni.2019.03.025 – volume: 107 start-page: 22534 year: 2010 ident: 8219_CR9 publication-title: Proc. Natl Acad. Sci. USA doi: 10.1073/pnas.0913805107 – volume: 183 start-page: 2020 year: 2020 ident: 8219_CR68 publication-title: Cell doi: 10.1016/j.cell.2020.11.024 – volume: 550 start-page: 128 year: 2017 ident: 8219_CR32 publication-title: Nature doi: 10.1038/nature24028 – volume: 164 start-page: 564 year: 2016 ident: 8219_CR49 publication-title: Cell doi: 10.1016/j.cell.2015.12.032 – volume: 81 start-page: 2166 year: 2021 ident: 8219_CR55 publication-title: Mol. Cell doi: 10.1016/j.molcel.2021.03.008 – ident: 8219_CR72 – volume: 6 start-page: 551 year: 2000 ident: 8219_CR28 publication-title: Mol. Cell doi: 10.1016/S1097-2765(00)00054-X – volume: 12 start-page: 599 year: 1998 ident: 8219_CR54 publication-title: Genes Dev. doi: 10.1101/gad.12.5.599 – volume: 29 start-page: 24 year: 2011 ident: 8219_CR75 publication-title: Nat. Biotechnol. doi: 10.1038/nbt.1754 – volume: 22 start-page: 2497 year: 2012 ident: 8219_CR2 publication-title: Genome Res. doi: 10.1101/gr.143008.112 – volume: 115 start-page: E601 year: 2018 ident: 8219_CR42 publication-title: Proc. Natl Acad. Sci. USA doi: 10.1073/pnas.1718426115 – volume: 208 start-page: 2747 year: 2011 ident: 8219_CR46 publication-title: J. Exp. Med. doi: 10.1084/jem.20111680 – volume: 8 start-page: 16 year: 2015 ident: 8219_CR50 publication-title: Epigenetics Chromatin doi: 10.1186/s13072-015-0009-5 – volume: 67 start-page: 411 year: 2017 ident: 8219_CR3 publication-title: Mol. Cell doi: 10.1016/j.molcel.2017.06.027 – volume: 583 start-page: 729 year: 2020 ident: 8219_CR4 publication-title: Nature doi: 10.1038/s41586-020-2528-x – volume: 4 start-page: e309 year: 2006 ident: 8219_CR33 publication-title: PLoS Biol. doi: 10.1371/journal.pbio.0040309 – volume: 17 start-page: 261 year: 2020 ident: 8219_CR73 publication-title: Nat. Methods doi: 10.1038/s41592-019-0686-2 – volume: 82 start-page: 677 year: 2022 ident: 8219_CR29 publication-title: Mol. Cell doi: 10.1016/j.molcel.2021.12.008 – volume: 48 start-page: 1193 year: 2016 ident: 8219_CR51 publication-title: Nat. Genet. doi: 10.1038/ng.3646 – volume: 214 start-page: 373 year: 1990 ident: 8219_CR7 publication-title: J. Mol. Biol. doi: 10.1016/0022-2836(90)90187-Q – ident: 8219_CR61 doi: 10.1101/2023.04.11.536490 – ident: 8219_CR27 doi: 10.1016/j.cell.2023.10.006 – volume: 49 start-page: 199 year: 2020 ident: 8219_CR59 publication-title: Annu. Rev. Biophys. doi: 10.1146/annurev-biophys-121219-081542 – volume: 10 year: 2019 ident: 8219_CR41 publication-title: Nat. Commun. doi: 10.1038/s41467-019-10970-y – volume: 79 start-page: 1129 year: 1982 ident: 8219_CR21 publication-title: Proc. Natl Acad. Sci. USA doi: 10.1073/pnas.79.4.1129 – ident: 8219_CR71 doi: 10.1101/2022.07.22.501078 – volume: 76 start-page: 480 year: 2015 ident: 8219_CR47 publication-title: Cytokine doi: 10.1016/j.cyto.2015.07.019 – volume: 368 start-page: 1449 year: 2020 ident: 8219_CR15 publication-title: Science doi: 10.1126/science.aaz1646 – volume: 10 year: 2009 ident: 8219_CR79 publication-title: Genome Biol. doi: 10.1186/gb-2009-10-3-r25 – volume: 13 start-page: 2369 year: 1999 ident: 8219_CR24 publication-title: Genes Dev. doi: 10.1101/gad.13.18.2369 – volume: 117 start-page: 2456 year: 2020 ident: 8219_CR60 publication-title: Proc. Natl Acad. Sci. USA doi: 10.1073/pnas.1911188117 – volume: 81 start-page: 255 year: 2021 ident: 8219_CR16 publication-title: Mol. Cell doi: 10.1016/j.molcel.2020.11.015 – volume: 13 start-page: 613 year: 2012 ident: 8219_CR1 publication-title: Nat. Rev. Genet. doi: 10.1038/nrg3207 – volume: 67 start-page: 833 year: 1991 ident: 8219_CR57 publication-title: Cell doi: 10.1016/0092-8674(91)90354-2 – ident: 8219_CR65 doi: 10.1038/s41588-024-01706-w – ident: 8219_CR82 doi: 10.5281/zenodo.13841007 – volume: 15 year: 2014 ident: 8219_CR77 publication-title: Genome Biol. doi: 10.1186/s13059-014-0550-8 – volume: 85 start-page: 382 year: 1988 ident: 8219_CR6 publication-title: Proc. Natl Acad. Sci. USA doi: 10.1073/pnas.85.2.382 – volume: 346 start-page: 135 year: 2005 ident: 8219_CR31 publication-title: J. Mol. Biol. doi: 10.1016/j.jmb.2004.11.056 – volume: 616 start-page: 365 year: 2023 ident: 8219_CR66 publication-title: Nature doi: 10.1038/s41586-023-05906-y – volume: 41 start-page: 488 year: 2023 ident: 8219_CR67 publication-title: Nat. Biotechnol. doi: 10.1038/s41587-022-01494-w – volume: 10 start-page: e64320 year: 2021 ident: 8219_CR36 publication-title: Elife doi: 10.7554/eLife.64320 – volume: 4 start-page: 1753 year: 1990 ident: 8219_CR39 publication-title: Genes Dev. doi: 10.1101/gad.4.10.1753 – volume: 43 start-page: 145 year: 2011 ident: 8219_CR10 publication-title: Mol. Cell doi: 10.1016/j.molcel.2011.06.016 – volume: 470 start-page: 279 year: 2011 ident: 8219_CR30 publication-title: Nature doi: 10.1038/nature09692 – volume: 33 start-page: 2497 year: 2013 ident: 8219_CR44 publication-title: Mol. Cell. Biol. doi: 10.1128/MCB.01180-12 – volume: 53 start-page: 279 year: 2021 ident: 8219_CR69 publication-title: Nat. Genet. doi: 10.1038/s41588-020-00768-w – volume: 17 start-page: 319 year: 2020 ident: 8219_CR14 publication-title: Nat. Methods doi: 10.1038/s41592-019-0730-2 – volume: 4 start-page: 649 year: 1999 ident: 8219_CR23 publication-title: Mol. Cell doi: 10.1016/S1097-2765(00)80216-6 – volume: 83 start-page: 1091 year: 1995 ident: 8219_CR8 publication-title: Cell doi: 10.1016/0092-8674(95)90136-1 – ident: 8219_CR83 doi: 10.5281/zenodo.13840888 – ident: 8219_CR56 doi: 10.1016/j.molcel.2023.12.004 – reference: 38352517 - bioRxiv. 2024 Feb 04:2024.02.02.578660. doi: 10.1101/2024.02.02.578660.
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Snippet	The binding of multiple transcription factors (TFs) to genomic enhancers drives gene expression in mammalian cells 1 . However, the molecular details that link... The binding of multiple transcription factors (TFs) to genomic enhancers drives gene expression in mammalian cells . However, the molecular details that link... The binding of multiple transcription factors (TFs) to genomic enhancers drives gene expression in mammalian cells'. However, the molecular details that link... The binding of multiple transcription factors (TFs) to genomic enhancers drives gene expression in mammalian cells1. However, the molecular details that link... The binding of multiple transcription factors (TFs) to genomic enhancers drives gene expression in mammalian cells. However, the molecular details that link...
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SubjectTerms	13 13/106 38 45/15 45/23 45/91 631/208/200 631/337/100 631/337/572 631/553/552 Binding Sites Chromatin DNA - genetics DNA - metabolism DNA Footprinting DNA Methylation Enhancer Elements, Genetic Enhancers Gene expression Gene Expression Regulation Humanities and Social Sciences Humans Interferon Type I - metabolism K562 Cells Kinetics Mammalian cells Models, Molecular multidisciplinary Nucleosomes Nucleosomes - genetics Nucleosomes - metabolism Nucleotide sequence Promoter Regions, Genetic Protein Binding Proteins Regulatory proteins Regulatory sequences Response Elements RNA polymerase Science Science (multidisciplinary) Single Molecule Imaging Statistical mechanics Thermodynamics Transcription factors Transcription Factors - metabolism
Title	Single-molecule states link transcription factor binding to gene expression
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