A Novel Allosteric Mechanism on Protein–DNA Interactions underlying the Phosphorylation-Dependent Regulation of Ets1 Target Gene Expressions
Cooperative assemblies of transcription factors (TFs) on target gene enhancers coordinate cell proliferation, fate specification, and differentiation through precise and complicated transcriptional mechanisms. Chemical modifications, such as phosphorylation, of TFs induced by cell signaling further...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Shiina, Masaaki [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2015transfer abstract |
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| Umfang: |
15 |
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| Übergeordnetes Werk: |
Enthalten in: Fabrication of chitin microspheres and their multipurpose application as catalyst support and adsorbent - Wang, Yuntao ELSEVIER, 2015, JMB, Amsterdam [u.a.] |
|---|---|
| Übergeordnetes Werk: |
volume:427 ; year:2015 ; number:8 ; day:24 ; month:04 ; pages:1655-1669 ; extent:15 |
| Links: |
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| DOI / URN: |
10.1016/j.jmb.2014.07.020 |
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ELV034948325 |
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| 520 | |a Cooperative assemblies of transcription factors (TFs) on target gene enhancers coordinate cell proliferation, fate specification, and differentiation through precise and complicated transcriptional mechanisms. Chemical modifications, such as phosphorylation, of TFs induced by cell signaling further modulate the dynamic cooperativity of TFs. In this study, we found that various Ets1-containing TF–DNA complexes respond differently to calcium-induced phosphorylation of Ets1, which is known to inhibit Ets1–DNA binding. Crystallographic analysis of a complex comprising Ets1, Runx1, and CBFβ at the TCRα enhancer revealed that Ets1 acquires robust binding stability in the Runx1 and DNA-complexed state, via allosteric mechanisms. This allows phosphorylated Ets1 to be retained at the TCRα enhancer with Runx1, in contrast to other Ets1 target gene enhancers including mb-1 and stromelysin-1. This study provides a structure-based model for cell-signaling-dependent regulation of target genes, mediated via chemical modification of TFs. | ||
| 520 | |a Cooperative assemblies of transcription factors (TFs) on target gene enhancers coordinate cell proliferation, fate specification, and differentiation through precise and complicated transcriptional mechanisms. Chemical modifications, such as phosphorylation, of TFs induced by cell signaling further modulate the dynamic cooperativity of TFs. In this study, we found that various Ets1-containing TF–DNA complexes respond differently to calcium-induced phosphorylation of Ets1, which is known to inhibit Ets1–DNA binding. Crystallographic analysis of a complex comprising Ets1, Runx1, and CBFβ at the TCRα enhancer revealed that Ets1 acquires robust binding stability in the Runx1 and DNA-complexed state, via allosteric mechanisms. This allows phosphorylated Ets1 to be retained at the TCRα enhancer with Runx1, in contrast to other Ets1 target gene enhancers including mb-1 and stromelysin-1. This study provides a structure-based model for cell-signaling-dependent regulation of target genes, mediated via chemical modification of TFs. | ||
| 700 | 1 | |a Hamada, Keisuke |4 oth | |
| 700 | 1 | |a Inoue-Bungo, Taiko |4 oth | |
| 700 | 1 | |a Shimamura, Mariko |4 oth | |
| 700 | 1 | |a Uchiyama, Akiko |4 oth | |
| 700 | 1 | |a Baba, Shiho |4 oth | |
| 700 | 1 | |a Sato, Ko |4 oth | |
| 700 | 1 | |a Yamamoto, Masaki |4 oth | |
| 700 | 1 | |a Ogata, Kazuhiro |4 oth | |
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10.1016/j.jmb.2014.07.020 doi GBVA2015022000021.pica (DE-627)ELV034948325 (ELSEVIER)S0022-2836(14)00368-4 DE-627 ger DE-627 rakwb eng 570 610 570 DE-600 610 DE-600 540 VZ 660 VZ 540 VZ BIODIV DE-30 fid 42.13 bkl Shiina, Masaaki verfasserin aut A Novel Allosteric Mechanism on Protein–DNA Interactions underlying the Phosphorylation-Dependent Regulation of Ets1 Target Gene Expressions 2015transfer abstract 15 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Cooperative assemblies of transcription factors (TFs) on target gene enhancers coordinate cell proliferation, fate specification, and differentiation through precise and complicated transcriptional mechanisms. Chemical modifications, such as phosphorylation, of TFs induced by cell signaling further modulate the dynamic cooperativity of TFs. In this study, we found that various Ets1-containing TF–DNA complexes respond differently to calcium-induced phosphorylation of Ets1, which is known to inhibit Ets1–DNA binding. Crystallographic analysis of a complex comprising Ets1, Runx1, and CBFβ at the TCRα enhancer revealed that Ets1 acquires robust binding stability in the Runx1 and DNA-complexed state, via allosteric mechanisms. This allows phosphorylated Ets1 to be retained at the TCRα enhancer with Runx1, in contrast to other Ets1 target gene enhancers including mb-1 and stromelysin-1. This study provides a structure-based model for cell-signaling-dependent regulation of target genes, mediated via chemical modification of TFs. Cooperative assemblies of transcription factors (TFs) on target gene enhancers coordinate cell proliferation, fate specification, and differentiation through precise and complicated transcriptional mechanisms. Chemical modifications, such as phosphorylation, of TFs induced by cell signaling further modulate the dynamic cooperativity of TFs. In this study, we found that various Ets1-containing TF–DNA complexes respond differently to calcium-induced phosphorylation of Ets1, which is known to inhibit Ets1–DNA binding. Crystallographic analysis of a complex comprising Ets1, Runx1, and CBFβ at the TCRα enhancer revealed that Ets1 acquires robust binding stability in the Runx1 and DNA-complexed state, via allosteric mechanisms. This allows phosphorylated Ets1 to be retained at the TCRα enhancer with Runx1, in contrast to other Ets1 target gene enhancers including mb-1 and stromelysin-1. This study provides a structure-based model for cell-signaling-dependent regulation of target genes, mediated via chemical modification of TFs. Hamada, Keisuke oth Inoue-Bungo, Taiko oth Shimamura, Mariko oth Uchiyama, Akiko oth Baba, Shiho oth Sato, Ko oth Yamamoto, Masaki oth Ogata, Kazuhiro oth Enthalten in Elsevier Wang, Yuntao ELSEVIER Fabrication of chitin microspheres and their multipurpose application as catalyst support and adsorbent 2015 JMB Amsterdam [u.a.] (DE-627)ELV012766127 volume:427 year:2015 number:8 day:24 month:04 pages:1655-1669 extent:15 https://doi.org/10.1016/j.jmb.2014.07.020 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U FID-BIODIV SSG-OLC-PHA GBV_ILN_40 42.13 Molekularbiologie VZ AR 427 2015 8 24 0424 1655-1669 15 045F 570 |
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10.1016/j.jmb.2014.07.020 doi GBVA2015022000021.pica (DE-627)ELV034948325 (ELSEVIER)S0022-2836(14)00368-4 DE-627 ger DE-627 rakwb eng 570 610 570 DE-600 610 DE-600 540 VZ 660 VZ 540 VZ BIODIV DE-30 fid 42.13 bkl Shiina, Masaaki verfasserin aut A Novel Allosteric Mechanism on Protein–DNA Interactions underlying the Phosphorylation-Dependent Regulation of Ets1 Target Gene Expressions 2015transfer abstract 15 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Cooperative assemblies of transcription factors (TFs) on target gene enhancers coordinate cell proliferation, fate specification, and differentiation through precise and complicated transcriptional mechanisms. Chemical modifications, such as phosphorylation, of TFs induced by cell signaling further modulate the dynamic cooperativity of TFs. In this study, we found that various Ets1-containing TF–DNA complexes respond differently to calcium-induced phosphorylation of Ets1, which is known to inhibit Ets1–DNA binding. Crystallographic analysis of a complex comprising Ets1, Runx1, and CBFβ at the TCRα enhancer revealed that Ets1 acquires robust binding stability in the Runx1 and DNA-complexed state, via allosteric mechanisms. This allows phosphorylated Ets1 to be retained at the TCRα enhancer with Runx1, in contrast to other Ets1 target gene enhancers including mb-1 and stromelysin-1. This study provides a structure-based model for cell-signaling-dependent regulation of target genes, mediated via chemical modification of TFs. Cooperative assemblies of transcription factors (TFs) on target gene enhancers coordinate cell proliferation, fate specification, and differentiation through precise and complicated transcriptional mechanisms. Chemical modifications, such as phosphorylation, of TFs induced by cell signaling further modulate the dynamic cooperativity of TFs. In this study, we found that various Ets1-containing TF–DNA complexes respond differently to calcium-induced phosphorylation of Ets1, which is known to inhibit Ets1–DNA binding. Crystallographic analysis of a complex comprising Ets1, Runx1, and CBFβ at the TCRα enhancer revealed that Ets1 acquires robust binding stability in the Runx1 and DNA-complexed state, via allosteric mechanisms. This allows phosphorylated Ets1 to be retained at the TCRα enhancer with Runx1, in contrast to other Ets1 target gene enhancers including mb-1 and stromelysin-1. This study provides a structure-based model for cell-signaling-dependent regulation of target genes, mediated via chemical modification of TFs. Hamada, Keisuke oth Inoue-Bungo, Taiko oth Shimamura, Mariko oth Uchiyama, Akiko oth Baba, Shiho oth Sato, Ko oth Yamamoto, Masaki oth Ogata, Kazuhiro oth Enthalten in Elsevier Wang, Yuntao ELSEVIER Fabrication of chitin microspheres and their multipurpose application as catalyst support and adsorbent 2015 JMB Amsterdam [u.a.] (DE-627)ELV012766127 volume:427 year:2015 number:8 day:24 month:04 pages:1655-1669 extent:15 https://doi.org/10.1016/j.jmb.2014.07.020 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U FID-BIODIV SSG-OLC-PHA GBV_ILN_40 42.13 Molekularbiologie VZ AR 427 2015 8 24 0424 1655-1669 15 045F 570 |
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10.1016/j.jmb.2014.07.020 doi GBVA2015022000021.pica (DE-627)ELV034948325 (ELSEVIER)S0022-2836(14)00368-4 DE-627 ger DE-627 rakwb eng 570 610 570 DE-600 610 DE-600 540 VZ 660 VZ 540 VZ BIODIV DE-30 fid 42.13 bkl Shiina, Masaaki verfasserin aut A Novel Allosteric Mechanism on Protein–DNA Interactions underlying the Phosphorylation-Dependent Regulation of Ets1 Target Gene Expressions 2015transfer abstract 15 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Cooperative assemblies of transcription factors (TFs) on target gene enhancers coordinate cell proliferation, fate specification, and differentiation through precise and complicated transcriptional mechanisms. Chemical modifications, such as phosphorylation, of TFs induced by cell signaling further modulate the dynamic cooperativity of TFs. In this study, we found that various Ets1-containing TF–DNA complexes respond differently to calcium-induced phosphorylation of Ets1, which is known to inhibit Ets1–DNA binding. Crystallographic analysis of a complex comprising Ets1, Runx1, and CBFβ at the TCRα enhancer revealed that Ets1 acquires robust binding stability in the Runx1 and DNA-complexed state, via allosteric mechanisms. This allows phosphorylated Ets1 to be retained at the TCRα enhancer with Runx1, in contrast to other Ets1 target gene enhancers including mb-1 and stromelysin-1. This study provides a structure-based model for cell-signaling-dependent regulation of target genes, mediated via chemical modification of TFs. Cooperative assemblies of transcription factors (TFs) on target gene enhancers coordinate cell proliferation, fate specification, and differentiation through precise and complicated transcriptional mechanisms. Chemical modifications, such as phosphorylation, of TFs induced by cell signaling further modulate the dynamic cooperativity of TFs. In this study, we found that various Ets1-containing TF–DNA complexes respond differently to calcium-induced phosphorylation of Ets1, which is known to inhibit Ets1–DNA binding. Crystallographic analysis of a complex comprising Ets1, Runx1, and CBFβ at the TCRα enhancer revealed that Ets1 acquires robust binding stability in the Runx1 and DNA-complexed state, via allosteric mechanisms. This allows phosphorylated Ets1 to be retained at the TCRα enhancer with Runx1, in contrast to other Ets1 target gene enhancers including mb-1 and stromelysin-1. This study provides a structure-based model for cell-signaling-dependent regulation of target genes, mediated via chemical modification of TFs. Hamada, Keisuke oth Inoue-Bungo, Taiko oth Shimamura, Mariko oth Uchiyama, Akiko oth Baba, Shiho oth Sato, Ko oth Yamamoto, Masaki oth Ogata, Kazuhiro oth Enthalten in Elsevier Wang, Yuntao ELSEVIER Fabrication of chitin microspheres and their multipurpose application as catalyst support and adsorbent 2015 JMB Amsterdam [u.a.] (DE-627)ELV012766127 volume:427 year:2015 number:8 day:24 month:04 pages:1655-1669 extent:15 https://doi.org/10.1016/j.jmb.2014.07.020 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U FID-BIODIV SSG-OLC-PHA GBV_ILN_40 42.13 Molekularbiologie VZ AR 427 2015 8 24 0424 1655-1669 15 045F 570 |
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10.1016/j.jmb.2014.07.020 doi GBVA2015022000021.pica (DE-627)ELV034948325 (ELSEVIER)S0022-2836(14)00368-4 DE-627 ger DE-627 rakwb eng 570 610 570 DE-600 610 DE-600 540 VZ 660 VZ 540 VZ BIODIV DE-30 fid 42.13 bkl Shiina, Masaaki verfasserin aut A Novel Allosteric Mechanism on Protein–DNA Interactions underlying the Phosphorylation-Dependent Regulation of Ets1 Target Gene Expressions 2015transfer abstract 15 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Cooperative assemblies of transcription factors (TFs) on target gene enhancers coordinate cell proliferation, fate specification, and differentiation through precise and complicated transcriptional mechanisms. Chemical modifications, such as phosphorylation, of TFs induced by cell signaling further modulate the dynamic cooperativity of TFs. In this study, we found that various Ets1-containing TF–DNA complexes respond differently to calcium-induced phosphorylation of Ets1, which is known to inhibit Ets1–DNA binding. Crystallographic analysis of a complex comprising Ets1, Runx1, and CBFβ at the TCRα enhancer revealed that Ets1 acquires robust binding stability in the Runx1 and DNA-complexed state, via allosteric mechanisms. This allows phosphorylated Ets1 to be retained at the TCRα enhancer with Runx1, in contrast to other Ets1 target gene enhancers including mb-1 and stromelysin-1. This study provides a structure-based model for cell-signaling-dependent regulation of target genes, mediated via chemical modification of TFs. Cooperative assemblies of transcription factors (TFs) on target gene enhancers coordinate cell proliferation, fate specification, and differentiation through precise and complicated transcriptional mechanisms. Chemical modifications, such as phosphorylation, of TFs induced by cell signaling further modulate the dynamic cooperativity of TFs. In this study, we found that various Ets1-containing TF–DNA complexes respond differently to calcium-induced phosphorylation of Ets1, which is known to inhibit Ets1–DNA binding. Crystallographic analysis of a complex comprising Ets1, Runx1, and CBFβ at the TCRα enhancer revealed that Ets1 acquires robust binding stability in the Runx1 and DNA-complexed state, via allosteric mechanisms. This allows phosphorylated Ets1 to be retained at the TCRα enhancer with Runx1, in contrast to other Ets1 target gene enhancers including mb-1 and stromelysin-1. This study provides a structure-based model for cell-signaling-dependent regulation of target genes, mediated via chemical modification of TFs. Hamada, Keisuke oth Inoue-Bungo, Taiko oth Shimamura, Mariko oth Uchiyama, Akiko oth Baba, Shiho oth Sato, Ko oth Yamamoto, Masaki oth Ogata, Kazuhiro oth Enthalten in Elsevier Wang, Yuntao ELSEVIER Fabrication of chitin microspheres and their multipurpose application as catalyst support and adsorbent 2015 JMB Amsterdam [u.a.] (DE-627)ELV012766127 volume:427 year:2015 number:8 day:24 month:04 pages:1655-1669 extent:15 https://doi.org/10.1016/j.jmb.2014.07.020 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U FID-BIODIV SSG-OLC-PHA GBV_ILN_40 42.13 Molekularbiologie VZ AR 427 2015 8 24 0424 1655-1669 15 045F 570 |
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10.1016/j.jmb.2014.07.020 doi GBVA2015022000021.pica (DE-627)ELV034948325 (ELSEVIER)S0022-2836(14)00368-4 DE-627 ger DE-627 rakwb eng 570 610 570 DE-600 610 DE-600 540 VZ 660 VZ 540 VZ BIODIV DE-30 fid 42.13 bkl Shiina, Masaaki verfasserin aut A Novel Allosteric Mechanism on Protein–DNA Interactions underlying the Phosphorylation-Dependent Regulation of Ets1 Target Gene Expressions 2015transfer abstract 15 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Cooperative assemblies of transcription factors (TFs) on target gene enhancers coordinate cell proliferation, fate specification, and differentiation through precise and complicated transcriptional mechanisms. Chemical modifications, such as phosphorylation, of TFs induced by cell signaling further modulate the dynamic cooperativity of TFs. In this study, we found that various Ets1-containing TF–DNA complexes respond differently to calcium-induced phosphorylation of Ets1, which is known to inhibit Ets1–DNA binding. Crystallographic analysis of a complex comprising Ets1, Runx1, and CBFβ at the TCRα enhancer revealed that Ets1 acquires robust binding stability in the Runx1 and DNA-complexed state, via allosteric mechanisms. This allows phosphorylated Ets1 to be retained at the TCRα enhancer with Runx1, in contrast to other Ets1 target gene enhancers including mb-1 and stromelysin-1. This study provides a structure-based model for cell-signaling-dependent regulation of target genes, mediated via chemical modification of TFs. Cooperative assemblies of transcription factors (TFs) on target gene enhancers coordinate cell proliferation, fate specification, and differentiation through precise and complicated transcriptional mechanisms. Chemical modifications, such as phosphorylation, of TFs induced by cell signaling further modulate the dynamic cooperativity of TFs. In this study, we found that various Ets1-containing TF–DNA complexes respond differently to calcium-induced phosphorylation of Ets1, which is known to inhibit Ets1–DNA binding. Crystallographic analysis of a complex comprising Ets1, Runx1, and CBFβ at the TCRα enhancer revealed that Ets1 acquires robust binding stability in the Runx1 and DNA-complexed state, via allosteric mechanisms. This allows phosphorylated Ets1 to be retained at the TCRα enhancer with Runx1, in contrast to other Ets1 target gene enhancers including mb-1 and stromelysin-1. This study provides a structure-based model for cell-signaling-dependent regulation of target genes, mediated via chemical modification of TFs. Hamada, Keisuke oth Inoue-Bungo, Taiko oth Shimamura, Mariko oth Uchiyama, Akiko oth Baba, Shiho oth Sato, Ko oth Yamamoto, Masaki oth Ogata, Kazuhiro oth Enthalten in Elsevier Wang, Yuntao ELSEVIER Fabrication of chitin microspheres and their multipurpose application as catalyst support and adsorbent 2015 JMB Amsterdam [u.a.] (DE-627)ELV012766127 volume:427 year:2015 number:8 day:24 month:04 pages:1655-1669 extent:15 https://doi.org/10.1016/j.jmb.2014.07.020 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U FID-BIODIV SSG-OLC-PHA GBV_ILN_40 42.13 Molekularbiologie VZ AR 427 2015 8 24 0424 1655-1669 15 045F 570 |
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Enthalten in Fabrication of chitin microspheres and their multipurpose application as catalyst support and adsorbent Amsterdam [u.a.] volume:427 year:2015 number:8 day:24 month:04 pages:1655-1669 extent:15 |
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Enthalten in Fabrication of chitin microspheres and their multipurpose application as catalyst support and adsorbent Amsterdam [u.a.] volume:427 year:2015 number:8 day:24 month:04 pages:1655-1669 extent:15 |
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Shiina, Masaaki @@aut@@ Hamada, Keisuke @@oth@@ Inoue-Bungo, Taiko @@oth@@ Shimamura, Mariko @@oth@@ Uchiyama, Akiko @@oth@@ Baba, Shiho @@oth@@ Sato, Ko @@oth@@ Yamamoto, Masaki @@oth@@ Ogata, Kazuhiro @@oth@@ |
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A Novel Allosteric Mechanism on Protein–DNA Interactions underlying the Phosphorylation-Dependent Regulation of Ets1 Target Gene Expressions |
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Cooperative assemblies of transcription factors (TFs) on target gene enhancers coordinate cell proliferation, fate specification, and differentiation through precise and complicated transcriptional mechanisms. Chemical modifications, such as phosphorylation, of TFs induced by cell signaling further modulate the dynamic cooperativity of TFs. In this study, we found that various Ets1-containing TF–DNA complexes respond differently to calcium-induced phosphorylation of Ets1, which is known to inhibit Ets1–DNA binding. Crystallographic analysis of a complex comprising Ets1, Runx1, and CBFβ at the TCRα enhancer revealed that Ets1 acquires robust binding stability in the Runx1 and DNA-complexed state, via allosteric mechanisms. This allows phosphorylated Ets1 to be retained at the TCRα enhancer with Runx1, in contrast to other Ets1 target gene enhancers including mb-1 and stromelysin-1. This study provides a structure-based model for cell-signaling-dependent regulation of target genes, mediated via chemical modification of TFs. |
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Cooperative assemblies of transcription factors (TFs) on target gene enhancers coordinate cell proliferation, fate specification, and differentiation through precise and complicated transcriptional mechanisms. Chemical modifications, such as phosphorylation, of TFs induced by cell signaling further modulate the dynamic cooperativity of TFs. In this study, we found that various Ets1-containing TF–DNA complexes respond differently to calcium-induced phosphorylation of Ets1, which is known to inhibit Ets1–DNA binding. Crystallographic analysis of a complex comprising Ets1, Runx1, and CBFβ at the TCRα enhancer revealed that Ets1 acquires robust binding stability in the Runx1 and DNA-complexed state, via allosteric mechanisms. This allows phosphorylated Ets1 to be retained at the TCRα enhancer with Runx1, in contrast to other Ets1 target gene enhancers including mb-1 and stromelysin-1. This study provides a structure-based model for cell-signaling-dependent regulation of target genes, mediated via chemical modification of TFs. |
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Cooperative assemblies of transcription factors (TFs) on target gene enhancers coordinate cell proliferation, fate specification, and differentiation through precise and complicated transcriptional mechanisms. Chemical modifications, such as phosphorylation, of TFs induced by cell signaling further modulate the dynamic cooperativity of TFs. In this study, we found that various Ets1-containing TF–DNA complexes respond differently to calcium-induced phosphorylation of Ets1, which is known to inhibit Ets1–DNA binding. Crystallographic analysis of a complex comprising Ets1, Runx1, and CBFβ at the TCRα enhancer revealed that Ets1 acquires robust binding stability in the Runx1 and DNA-complexed state, via allosteric mechanisms. This allows phosphorylated Ets1 to be retained at the TCRα enhancer with Runx1, in contrast to other Ets1 target gene enhancers including mb-1 and stromelysin-1. This study provides a structure-based model for cell-signaling-dependent regulation of target genes, mediated via chemical modification of TFs. |
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