ID: 188
Recently, it has been shown that substitution of alanine for phenylalanine 77 in the N-domain of STAT1 (signal transducer and activator of transcription (1) prevents cooperative binding of tetramers on DNA and severely impairs transcriptional responses upon stimulation of cells with interferon-gamma...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Staab, Julia [verfasserIn] |
|---|
| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2015transfer abstract |
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| Übergeordnetes Werk: |
Enthalten in: The minimal clinically important differences of the Simple Shoulder Test are different for different arthroplasty types - McLaughlin, Richard J. ELSEVIER, 2022, the official journal of the International Cytokine Society, Oxford [u.a.] |
|---|---|
| Übergeordnetes Werk: |
volume:76 ; year:2015 ; number:1 ; pages:98 |
| Links: |
|---|
| DOI / URN: |
10.1016/j.cyto.2015.08.193 |
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| 520 | |a Recently, it has been shown that substitution of alanine for phenylalanine 77 in the N-domain of STAT1 (signal transducer and activator of transcription (1) prevents cooperative binding of tetramers on DNA and severely impairs transcriptional responses upon stimulation of cells with interferon-gamma (IFN-gamma). Cooperative DNA binding is the basis of efficient switching between non-occupied and occupied promoter states. In this study, we generated N-terminal mutants of STAT1 which showed improved tetramer stability on DNA. We identified two negatively charged N-terminal residues in each protomer of dimeric STAT1 which are required for the dissociation of higher-order oligomers on DNA. Similarly to the STAT1 mutant with impaired tetramerization, these N-terminal mutants showed elevated tyrosine-phosphorylation levels and prolonged nuclear accumulation upon stimulation of cells with IFN-gamma. Unlike the global impairment of IFN-gamma signalling in the tetramerization-deficient mutant, improved tetramer stability of the N-terminal mutants affected transcription in a promoter-specific manner and resulted in a distinct gene expression pattern. In summary, using these mutants we have gained a new mechanistic insight into how protein-DNA interactions regulate STAT1-mediated target gene recognition. While one side of the N-terminal dimer is crucial for the formation of tetrameric complexes on IFN-gamma-regulated promoters, the other side localized in close contact to the longitudinal axis of DNA has a rather inhibitory effect on the formation of higher-order oligomers, simply by disrupting cooperative DNA binding. | ||
| 520 | |a Recently, it has been shown that substitution of alanine for phenylalanine 77 in the N-domain of STAT1 (signal transducer and activator of transcription (1) prevents cooperative binding of tetramers on DNA and severely impairs transcriptional responses upon stimulation of cells with interferon-gamma (IFN-gamma). Cooperative DNA binding is the basis of efficient switching between non-occupied and occupied promoter states. In this study, we generated N-terminal mutants of STAT1 which showed improved tetramer stability on DNA. We identified two negatively charged N-terminal residues in each protomer of dimeric STAT1 which are required for the dissociation of higher-order oligomers on DNA. Similarly to the STAT1 mutant with impaired tetramerization, these N-terminal mutants showed elevated tyrosine-phosphorylation levels and prolonged nuclear accumulation upon stimulation of cells with IFN-gamma. Unlike the global impairment of IFN-gamma signalling in the tetramerization-deficient mutant, improved tetramer stability of the N-terminal mutants affected transcription in a promoter-specific manner and resulted in a distinct gene expression pattern. In summary, using these mutants we have gained a new mechanistic insight into how protein-DNA interactions regulate STAT1-mediated target gene recognition. While one side of the N-terminal dimer is crucial for the formation of tetrameric complexes on IFN-gamma-regulated promoters, the other side localized in close contact to the longitudinal axis of DNA has a rather inhibitory effect on the formation of higher-order oligomers, simply by disrupting cooperative DNA binding. | ||
| 700 | 1 | |a Riebeling, Theresa |4 oth | |
| 700 | 1 | |a Herrmann-Lingen, Christoph |4 oth | |
| 700 | 1 | |a Meyer, Thomas |4 oth | |
| 773 | 0 | 8 | |i Enthalten in |n Elsevier |a McLaughlin, Richard J. ELSEVIER |t The minimal clinically important differences of the Simple Shoulder Test are different for different arthroplasty types |d 2022 |d the official journal of the International Cytokine Society |g Oxford [u.a.] |w (DE-627)ELV008219540 |
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10.1016/j.cyto.2015.08.193 doi GBVA2015017000008.pica (DE-627)ELV018713548 (ELSEVIER)S1043-4666(15)00459-7 DE-627 ger DE-627 rakwb eng 570 570 DE-600 610 VZ 44.83 bkl Staab, Julia verfasserin aut ID: 188 2015transfer abstract nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Recently, it has been shown that substitution of alanine for phenylalanine 77 in the N-domain of STAT1 (signal transducer and activator of transcription (1) prevents cooperative binding of tetramers on DNA and severely impairs transcriptional responses upon stimulation of cells with interferon-gamma (IFN-gamma). Cooperative DNA binding is the basis of efficient switching between non-occupied and occupied promoter states. In this study, we generated N-terminal mutants of STAT1 which showed improved tetramer stability on DNA. We identified two negatively charged N-terminal residues in each protomer of dimeric STAT1 which are required for the dissociation of higher-order oligomers on DNA. Similarly to the STAT1 mutant with impaired tetramerization, these N-terminal mutants showed elevated tyrosine-phosphorylation levels and prolonged nuclear accumulation upon stimulation of cells with IFN-gamma. Unlike the global impairment of IFN-gamma signalling in the tetramerization-deficient mutant, improved tetramer stability of the N-terminal mutants affected transcription in a promoter-specific manner and resulted in a distinct gene expression pattern. In summary, using these mutants we have gained a new mechanistic insight into how protein-DNA interactions regulate STAT1-mediated target gene recognition. While one side of the N-terminal dimer is crucial for the formation of tetrameric complexes on IFN-gamma-regulated promoters, the other side localized in close contact to the longitudinal axis of DNA has a rather inhibitory effect on the formation of higher-order oligomers, simply by disrupting cooperative DNA binding. Recently, it has been shown that substitution of alanine for phenylalanine 77 in the N-domain of STAT1 (signal transducer and activator of transcription (1) prevents cooperative binding of tetramers on DNA and severely impairs transcriptional responses upon stimulation of cells with interferon-gamma (IFN-gamma). Cooperative DNA binding is the basis of efficient switching between non-occupied and occupied promoter states. In this study, we generated N-terminal mutants of STAT1 which showed improved tetramer stability on DNA. We identified two negatively charged N-terminal residues in each protomer of dimeric STAT1 which are required for the dissociation of higher-order oligomers on DNA. Similarly to the STAT1 mutant with impaired tetramerization, these N-terminal mutants showed elevated tyrosine-phosphorylation levels and prolonged nuclear accumulation upon stimulation of cells with IFN-gamma. Unlike the global impairment of IFN-gamma signalling in the tetramerization-deficient mutant, improved tetramer stability of the N-terminal mutants affected transcription in a promoter-specific manner and resulted in a distinct gene expression pattern. In summary, using these mutants we have gained a new mechanistic insight into how protein-DNA interactions regulate STAT1-mediated target gene recognition. While one side of the N-terminal dimer is crucial for the formation of tetrameric complexes on IFN-gamma-regulated promoters, the other side localized in close contact to the longitudinal axis of DNA has a rather inhibitory effect on the formation of higher-order oligomers, simply by disrupting cooperative DNA binding. Riebeling, Theresa oth Herrmann-Lingen, Christoph oth Meyer, Thomas oth Enthalten in Elsevier McLaughlin, Richard J. ELSEVIER The minimal clinically important differences of the Simple Shoulder Test are different for different arthroplasty types 2022 the official journal of the International Cytokine Society Oxford [u.a.] (DE-627)ELV008219540 volume:76 year:2015 number:1 pages:98 https://doi.org/10.1016/j.cyto.2015.08.193 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA 44.83 Rheumatologie Orthopädie VZ AR 76 2015 1 98 045F 570 |
| spelling |
10.1016/j.cyto.2015.08.193 doi GBVA2015017000008.pica (DE-627)ELV018713548 (ELSEVIER)S1043-4666(15)00459-7 DE-627 ger DE-627 rakwb eng 570 570 DE-600 610 VZ 44.83 bkl Staab, Julia verfasserin aut ID: 188 2015transfer abstract nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Recently, it has been shown that substitution of alanine for phenylalanine 77 in the N-domain of STAT1 (signal transducer and activator of transcription (1) prevents cooperative binding of tetramers on DNA and severely impairs transcriptional responses upon stimulation of cells with interferon-gamma (IFN-gamma). Cooperative DNA binding is the basis of efficient switching between non-occupied and occupied promoter states. In this study, we generated N-terminal mutants of STAT1 which showed improved tetramer stability on DNA. We identified two negatively charged N-terminal residues in each protomer of dimeric STAT1 which are required for the dissociation of higher-order oligomers on DNA. Similarly to the STAT1 mutant with impaired tetramerization, these N-terminal mutants showed elevated tyrosine-phosphorylation levels and prolonged nuclear accumulation upon stimulation of cells with IFN-gamma. Unlike the global impairment of IFN-gamma signalling in the tetramerization-deficient mutant, improved tetramer stability of the N-terminal mutants affected transcription in a promoter-specific manner and resulted in a distinct gene expression pattern. In summary, using these mutants we have gained a new mechanistic insight into how protein-DNA interactions regulate STAT1-mediated target gene recognition. While one side of the N-terminal dimer is crucial for the formation of tetrameric complexes on IFN-gamma-regulated promoters, the other side localized in close contact to the longitudinal axis of DNA has a rather inhibitory effect on the formation of higher-order oligomers, simply by disrupting cooperative DNA binding. Recently, it has been shown that substitution of alanine for phenylalanine 77 in the N-domain of STAT1 (signal transducer and activator of transcription (1) prevents cooperative binding of tetramers on DNA and severely impairs transcriptional responses upon stimulation of cells with interferon-gamma (IFN-gamma). Cooperative DNA binding is the basis of efficient switching between non-occupied and occupied promoter states. In this study, we generated N-terminal mutants of STAT1 which showed improved tetramer stability on DNA. We identified two negatively charged N-terminal residues in each protomer of dimeric STAT1 which are required for the dissociation of higher-order oligomers on DNA. Similarly to the STAT1 mutant with impaired tetramerization, these N-terminal mutants showed elevated tyrosine-phosphorylation levels and prolonged nuclear accumulation upon stimulation of cells with IFN-gamma. Unlike the global impairment of IFN-gamma signalling in the tetramerization-deficient mutant, improved tetramer stability of the N-terminal mutants affected transcription in a promoter-specific manner and resulted in a distinct gene expression pattern. In summary, using these mutants we have gained a new mechanistic insight into how protein-DNA interactions regulate STAT1-mediated target gene recognition. While one side of the N-terminal dimer is crucial for the formation of tetrameric complexes on IFN-gamma-regulated promoters, the other side localized in close contact to the longitudinal axis of DNA has a rather inhibitory effect on the formation of higher-order oligomers, simply by disrupting cooperative DNA binding. Riebeling, Theresa oth Herrmann-Lingen, Christoph oth Meyer, Thomas oth Enthalten in Elsevier McLaughlin, Richard J. ELSEVIER The minimal clinically important differences of the Simple Shoulder Test are different for different arthroplasty types 2022 the official journal of the International Cytokine Society Oxford [u.a.] (DE-627)ELV008219540 volume:76 year:2015 number:1 pages:98 https://doi.org/10.1016/j.cyto.2015.08.193 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA 44.83 Rheumatologie Orthopädie VZ AR 76 2015 1 98 045F 570 |
| allfields_unstemmed |
10.1016/j.cyto.2015.08.193 doi GBVA2015017000008.pica (DE-627)ELV018713548 (ELSEVIER)S1043-4666(15)00459-7 DE-627 ger DE-627 rakwb eng 570 570 DE-600 610 VZ 44.83 bkl Staab, Julia verfasserin aut ID: 188 2015transfer abstract nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Recently, it has been shown that substitution of alanine for phenylalanine 77 in the N-domain of STAT1 (signal transducer and activator of transcription (1) prevents cooperative binding of tetramers on DNA and severely impairs transcriptional responses upon stimulation of cells with interferon-gamma (IFN-gamma). Cooperative DNA binding is the basis of efficient switching between non-occupied and occupied promoter states. In this study, we generated N-terminal mutants of STAT1 which showed improved tetramer stability on DNA. We identified two negatively charged N-terminal residues in each protomer of dimeric STAT1 which are required for the dissociation of higher-order oligomers on DNA. Similarly to the STAT1 mutant with impaired tetramerization, these N-terminal mutants showed elevated tyrosine-phosphorylation levels and prolonged nuclear accumulation upon stimulation of cells with IFN-gamma. Unlike the global impairment of IFN-gamma signalling in the tetramerization-deficient mutant, improved tetramer stability of the N-terminal mutants affected transcription in a promoter-specific manner and resulted in a distinct gene expression pattern. In summary, using these mutants we have gained a new mechanistic insight into how protein-DNA interactions regulate STAT1-mediated target gene recognition. While one side of the N-terminal dimer is crucial for the formation of tetrameric complexes on IFN-gamma-regulated promoters, the other side localized in close contact to the longitudinal axis of DNA has a rather inhibitory effect on the formation of higher-order oligomers, simply by disrupting cooperative DNA binding. Recently, it has been shown that substitution of alanine for phenylalanine 77 in the N-domain of STAT1 (signal transducer and activator of transcription (1) prevents cooperative binding of tetramers on DNA and severely impairs transcriptional responses upon stimulation of cells with interferon-gamma (IFN-gamma). Cooperative DNA binding is the basis of efficient switching between non-occupied and occupied promoter states. In this study, we generated N-terminal mutants of STAT1 which showed improved tetramer stability on DNA. We identified two negatively charged N-terminal residues in each protomer of dimeric STAT1 which are required for the dissociation of higher-order oligomers on DNA. Similarly to the STAT1 mutant with impaired tetramerization, these N-terminal mutants showed elevated tyrosine-phosphorylation levels and prolonged nuclear accumulation upon stimulation of cells with IFN-gamma. Unlike the global impairment of IFN-gamma signalling in the tetramerization-deficient mutant, improved tetramer stability of the N-terminal mutants affected transcription in a promoter-specific manner and resulted in a distinct gene expression pattern. In summary, using these mutants we have gained a new mechanistic insight into how protein-DNA interactions regulate STAT1-mediated target gene recognition. While one side of the N-terminal dimer is crucial for the formation of tetrameric complexes on IFN-gamma-regulated promoters, the other side localized in close contact to the longitudinal axis of DNA has a rather inhibitory effect on the formation of higher-order oligomers, simply by disrupting cooperative DNA binding. Riebeling, Theresa oth Herrmann-Lingen, Christoph oth Meyer, Thomas oth Enthalten in Elsevier McLaughlin, Richard J. ELSEVIER The minimal clinically important differences of the Simple Shoulder Test are different for different arthroplasty types 2022 the official journal of the International Cytokine Society Oxford [u.a.] (DE-627)ELV008219540 volume:76 year:2015 number:1 pages:98 https://doi.org/10.1016/j.cyto.2015.08.193 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA 44.83 Rheumatologie Orthopädie VZ AR 76 2015 1 98 045F 570 |
| allfieldsGer |
10.1016/j.cyto.2015.08.193 doi GBVA2015017000008.pica (DE-627)ELV018713548 (ELSEVIER)S1043-4666(15)00459-7 DE-627 ger DE-627 rakwb eng 570 570 DE-600 610 VZ 44.83 bkl Staab, Julia verfasserin aut ID: 188 2015transfer abstract nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Recently, it has been shown that substitution of alanine for phenylalanine 77 in the N-domain of STAT1 (signal transducer and activator of transcription (1) prevents cooperative binding of tetramers on DNA and severely impairs transcriptional responses upon stimulation of cells with interferon-gamma (IFN-gamma). Cooperative DNA binding is the basis of efficient switching between non-occupied and occupied promoter states. In this study, we generated N-terminal mutants of STAT1 which showed improved tetramer stability on DNA. We identified two negatively charged N-terminal residues in each protomer of dimeric STAT1 which are required for the dissociation of higher-order oligomers on DNA. Similarly to the STAT1 mutant with impaired tetramerization, these N-terminal mutants showed elevated tyrosine-phosphorylation levels and prolonged nuclear accumulation upon stimulation of cells with IFN-gamma. Unlike the global impairment of IFN-gamma signalling in the tetramerization-deficient mutant, improved tetramer stability of the N-terminal mutants affected transcription in a promoter-specific manner and resulted in a distinct gene expression pattern. In summary, using these mutants we have gained a new mechanistic insight into how protein-DNA interactions regulate STAT1-mediated target gene recognition. While one side of the N-terminal dimer is crucial for the formation of tetrameric complexes on IFN-gamma-regulated promoters, the other side localized in close contact to the longitudinal axis of DNA has a rather inhibitory effect on the formation of higher-order oligomers, simply by disrupting cooperative DNA binding. Recently, it has been shown that substitution of alanine for phenylalanine 77 in the N-domain of STAT1 (signal transducer and activator of transcription (1) prevents cooperative binding of tetramers on DNA and severely impairs transcriptional responses upon stimulation of cells with interferon-gamma (IFN-gamma). Cooperative DNA binding is the basis of efficient switching between non-occupied and occupied promoter states. In this study, we generated N-terminal mutants of STAT1 which showed improved tetramer stability on DNA. We identified two negatively charged N-terminal residues in each protomer of dimeric STAT1 which are required for the dissociation of higher-order oligomers on DNA. Similarly to the STAT1 mutant with impaired tetramerization, these N-terminal mutants showed elevated tyrosine-phosphorylation levels and prolonged nuclear accumulation upon stimulation of cells with IFN-gamma. Unlike the global impairment of IFN-gamma signalling in the tetramerization-deficient mutant, improved tetramer stability of the N-terminal mutants affected transcription in a promoter-specific manner and resulted in a distinct gene expression pattern. In summary, using these mutants we have gained a new mechanistic insight into how protein-DNA interactions regulate STAT1-mediated target gene recognition. While one side of the N-terminal dimer is crucial for the formation of tetrameric complexes on IFN-gamma-regulated promoters, the other side localized in close contact to the longitudinal axis of DNA has a rather inhibitory effect on the formation of higher-order oligomers, simply by disrupting cooperative DNA binding. Riebeling, Theresa oth Herrmann-Lingen, Christoph oth Meyer, Thomas oth Enthalten in Elsevier McLaughlin, Richard J. ELSEVIER The minimal clinically important differences of the Simple Shoulder Test are different for different arthroplasty types 2022 the official journal of the International Cytokine Society Oxford [u.a.] (DE-627)ELV008219540 volume:76 year:2015 number:1 pages:98 https://doi.org/10.1016/j.cyto.2015.08.193 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA 44.83 Rheumatologie Orthopädie VZ AR 76 2015 1 98 045F 570 |
| allfieldsSound |
10.1016/j.cyto.2015.08.193 doi GBVA2015017000008.pica (DE-627)ELV018713548 (ELSEVIER)S1043-4666(15)00459-7 DE-627 ger DE-627 rakwb eng 570 570 DE-600 610 VZ 44.83 bkl Staab, Julia verfasserin aut ID: 188 2015transfer abstract nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Recently, it has been shown that substitution of alanine for phenylalanine 77 in the N-domain of STAT1 (signal transducer and activator of transcription (1) prevents cooperative binding of tetramers on DNA and severely impairs transcriptional responses upon stimulation of cells with interferon-gamma (IFN-gamma). Cooperative DNA binding is the basis of efficient switching between non-occupied and occupied promoter states. In this study, we generated N-terminal mutants of STAT1 which showed improved tetramer stability on DNA. We identified two negatively charged N-terminal residues in each protomer of dimeric STAT1 which are required for the dissociation of higher-order oligomers on DNA. Similarly to the STAT1 mutant with impaired tetramerization, these N-terminal mutants showed elevated tyrosine-phosphorylation levels and prolonged nuclear accumulation upon stimulation of cells with IFN-gamma. Unlike the global impairment of IFN-gamma signalling in the tetramerization-deficient mutant, improved tetramer stability of the N-terminal mutants affected transcription in a promoter-specific manner and resulted in a distinct gene expression pattern. In summary, using these mutants we have gained a new mechanistic insight into how protein-DNA interactions regulate STAT1-mediated target gene recognition. While one side of the N-terminal dimer is crucial for the formation of tetrameric complexes on IFN-gamma-regulated promoters, the other side localized in close contact to the longitudinal axis of DNA has a rather inhibitory effect on the formation of higher-order oligomers, simply by disrupting cooperative DNA binding. Recently, it has been shown that substitution of alanine for phenylalanine 77 in the N-domain of STAT1 (signal transducer and activator of transcription (1) prevents cooperative binding of tetramers on DNA and severely impairs transcriptional responses upon stimulation of cells with interferon-gamma (IFN-gamma). Cooperative DNA binding is the basis of efficient switching between non-occupied and occupied promoter states. In this study, we generated N-terminal mutants of STAT1 which showed improved tetramer stability on DNA. We identified two negatively charged N-terminal residues in each protomer of dimeric STAT1 which are required for the dissociation of higher-order oligomers on DNA. Similarly to the STAT1 mutant with impaired tetramerization, these N-terminal mutants showed elevated tyrosine-phosphorylation levels and prolonged nuclear accumulation upon stimulation of cells with IFN-gamma. Unlike the global impairment of IFN-gamma signalling in the tetramerization-deficient mutant, improved tetramer stability of the N-terminal mutants affected transcription in a promoter-specific manner and resulted in a distinct gene expression pattern. In summary, using these mutants we have gained a new mechanistic insight into how protein-DNA interactions regulate STAT1-mediated target gene recognition. While one side of the N-terminal dimer is crucial for the formation of tetrameric complexes on IFN-gamma-regulated promoters, the other side localized in close contact to the longitudinal axis of DNA has a rather inhibitory effect on the formation of higher-order oligomers, simply by disrupting cooperative DNA binding. Riebeling, Theresa oth Herrmann-Lingen, Christoph oth Meyer, Thomas oth Enthalten in Elsevier McLaughlin, Richard J. ELSEVIER The minimal clinically important differences of the Simple Shoulder Test are different for different arthroplasty types 2022 the official journal of the International Cytokine Society Oxford [u.a.] (DE-627)ELV008219540 volume:76 year:2015 number:1 pages:98 https://doi.org/10.1016/j.cyto.2015.08.193 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA 44.83 Rheumatologie Orthopädie VZ AR 76 2015 1 98 045F 570 |
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Enthalten in The minimal clinically important differences of the Simple Shoulder Test are different for different arthroplasty types Oxford [u.a.] volume:76 year:2015 number:1 pages:98 |
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Enthalten in The minimal clinically important differences of the Simple Shoulder Test are different for different arthroplasty types Oxford [u.a.] volume:76 year:2015 number:1 pages:98 |
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The minimal clinically important differences of the Simple Shoulder Test are different for different arthroplasty types |
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Cooperative DNA binding is the basis of efficient switching between non-occupied and occupied promoter states. In this study, we generated N-terminal mutants of STAT1 which showed improved tetramer stability on DNA. We identified two negatively charged N-terminal residues in each protomer of dimeric STAT1 which are required for the dissociation of higher-order oligomers on DNA. Similarly to the STAT1 mutant with impaired tetramerization, these N-terminal mutants showed elevated tyrosine-phosphorylation levels and prolonged nuclear accumulation upon stimulation of cells with IFN-gamma. Unlike the global impairment of IFN-gamma signalling in the tetramerization-deficient mutant, improved tetramer stability of the N-terminal mutants affected transcription in a promoter-specific manner and resulted in a distinct gene expression pattern. 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Recently, it has been shown that substitution of alanine for phenylalanine 77 in the N-domain of STAT1 (signal transducer and activator of transcription (1) prevents cooperative binding of tetramers on DNA and severely impairs transcriptional responses upon stimulation of cells with interferon-gamma (IFN-gamma). Cooperative DNA binding is the basis of efficient switching between non-occupied and occupied promoter states. In this study, we generated N-terminal mutants of STAT1 which showed improved tetramer stability on DNA. We identified two negatively charged N-terminal residues in each protomer of dimeric STAT1 which are required for the dissociation of higher-order oligomers on DNA. Similarly to the STAT1 mutant with impaired tetramerization, these N-terminal mutants showed elevated tyrosine-phosphorylation levels and prolonged nuclear accumulation upon stimulation of cells with IFN-gamma. Unlike the global impairment of IFN-gamma signalling in the tetramerization-deficient mutant, improved tetramer stability of the N-terminal mutants affected transcription in a promoter-specific manner and resulted in a distinct gene expression pattern. In summary, using these mutants we have gained a new mechanistic insight into how protein-DNA interactions regulate STAT1-mediated target gene recognition. While one side of the N-terminal dimer is crucial for the formation of tetrameric complexes on IFN-gamma-regulated promoters, the other side localized in close contact to the longitudinal axis of DNA has a rather inhibitory effect on the formation of higher-order oligomers, simply by disrupting cooperative DNA binding. |
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Recently, it has been shown that substitution of alanine for phenylalanine 77 in the N-domain of STAT1 (signal transducer and activator of transcription (1) prevents cooperative binding of tetramers on DNA and severely impairs transcriptional responses upon stimulation of cells with interferon-gamma (IFN-gamma). Cooperative DNA binding is the basis of efficient switching between non-occupied and occupied promoter states. In this study, we generated N-terminal mutants of STAT1 which showed improved tetramer stability on DNA. We identified two negatively charged N-terminal residues in each protomer of dimeric STAT1 which are required for the dissociation of higher-order oligomers on DNA. Similarly to the STAT1 mutant with impaired tetramerization, these N-terminal mutants showed elevated tyrosine-phosphorylation levels and prolonged nuclear accumulation upon stimulation of cells with IFN-gamma. Unlike the global impairment of IFN-gamma signalling in the tetramerization-deficient mutant, improved tetramer stability of the N-terminal mutants affected transcription in a promoter-specific manner and resulted in a distinct gene expression pattern. In summary, using these mutants we have gained a new mechanistic insight into how protein-DNA interactions regulate STAT1-mediated target gene recognition. While one side of the N-terminal dimer is crucial for the formation of tetrameric complexes on IFN-gamma-regulated promoters, the other side localized in close contact to the longitudinal axis of DNA has a rather inhibitory effect on the formation of higher-order oligomers, simply by disrupting cooperative DNA binding. |
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Recently, it has been shown that substitution of alanine for phenylalanine 77 in the N-domain of STAT1 (signal transducer and activator of transcription (1) prevents cooperative binding of tetramers on DNA and severely impairs transcriptional responses upon stimulation of cells with interferon-gamma (IFN-gamma). Cooperative DNA binding is the basis of efficient switching between non-occupied and occupied promoter states. In this study, we generated N-terminal mutants of STAT1 which showed improved tetramer stability on DNA. We identified two negatively charged N-terminal residues in each protomer of dimeric STAT1 which are required for the dissociation of higher-order oligomers on DNA. Similarly to the STAT1 mutant with impaired tetramerization, these N-terminal mutants showed elevated tyrosine-phosphorylation levels and prolonged nuclear accumulation upon stimulation of cells with IFN-gamma. Unlike the global impairment of IFN-gamma signalling in the tetramerization-deficient mutant, improved tetramer stability of the N-terminal mutants affected transcription in a promoter-specific manner and resulted in a distinct gene expression pattern. In summary, using these mutants we have gained a new mechanistic insight into how protein-DNA interactions regulate STAT1-mediated target gene recognition. While one side of the N-terminal dimer is crucial for the formation of tetrameric complexes on IFN-gamma-regulated promoters, the other side localized in close contact to the longitudinal axis of DNA has a rather inhibitory effect on the formation of higher-order oligomers, simply by disrupting cooperative DNA binding. |
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