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Structural Motif of the GCN4 DNA Binding Domain Characterized by Affinity Cleaving
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| Zeitschriftentitel: | Science |
|---|---|
| Personen und Körperschaften: | , |
| In: | Science, 248, 1990, 4957, S. 847-850 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
American Association for the Advancement of Science (AAAS)
|
| Schlagwörter: |
| author_facet |
Oakley, Martha G. Dervan, Peter B. Oakley, Martha G. Dervan, Peter B. |
|---|---|
| author |
Oakley, Martha G. Dervan, Peter B. |
| spellingShingle |
Oakley, Martha G. Dervan, Peter B. Science Structural Motif of the GCN4 DNA Binding Domain Characterized by Affinity Cleaving Multidisciplinary |
| author_sort |
oakley, martha g. |
| spelling |
Oakley, Martha G. Dervan, Peter B. 0036-8075 1095-9203 American Association for the Advancement of Science (AAAS) Multidisciplinary http://dx.doi.org/10.1126/science.2111578 <jats:p> The NH2-terminal locations of a dimer containing the DNA binding domain of the yeast transcriptional activator GCN4 have been mapped on the binding sites 5′-CTGACTAAT-3′ and 5′-ATGACTCTT-3′. Affinity cleaving was effected by synthetic GCN4 proteins with Fe⋅EDTA moieties at the NH <jats:sub>2</jats:sub> -terminus. Analysis of the DNA cleavage patterns for dimers of the Fe⋅EDTA-proteins corresponding to GCN4 residues 222 to 281 and 226 to 281 revealed that the NH <jats:sub>2</jats:sub> -termini were in the major groove nine to ten base pairs apart and were symmetrically displaced four to five base pairs from the central C of the recognition site. This result is consistent with the Y-shaped scissor grip-leucine zipper model recently proposed for a class of DNA binding proteins important in the regulation of gene expression. </jats:p> Structural Motif of the GCN4 DNA Binding Domain Characterized by Affinity Cleaving Science |
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10.1126/science.2111578 |
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American Association for the Advancement of Science (AAAS), 1990 |
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American Association for the Advancement of Science (AAAS), 1990 |
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0036-8075 1095-9203 |
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1990 |
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American Association for the Advancement of Science (AAAS) |
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Science |
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49 |
| title |
Structural Motif of the GCN4 DNA Binding Domain Characterized by Affinity Cleaving |
| title_unstemmed |
Structural Motif of the GCN4 DNA Binding Domain Characterized by Affinity Cleaving |
| title_full |
Structural Motif of the GCN4 DNA Binding Domain Characterized by Affinity Cleaving |
| title_fullStr |
Structural Motif of the GCN4 DNA Binding Domain Characterized by Affinity Cleaving |
| title_full_unstemmed |
Structural Motif of the GCN4 DNA Binding Domain Characterized by Affinity Cleaving |
| title_short |
Structural Motif of the GCN4 DNA Binding Domain Characterized by Affinity Cleaving |
| title_sort |
structural motif of the gcn4 dna binding domain characterized by affinity cleaving |
| topic |
Multidisciplinary |
| url |
http://dx.doi.org/10.1126/science.2111578 |
| publishDate |
1990 |
| physical |
847-850 |
| description |
<jats:p>
The NH2-terminal locations of a dimer containing the DNA binding domain of the yeast transcriptional activator GCN4 have been mapped on the binding sites 5′-CTGACTAAT-3′ and 5′-ATGACTCTT-3′. Affinity cleaving was effected by synthetic GCN4 proteins with Fe⋅EDTA moieties at the NH
<jats:sub>2</jats:sub>
-terminus. Analysis of the DNA cleavage patterns for dimers of the Fe⋅EDTA-proteins corresponding to GCN4 residues 222 to 281 and 226 to 281 revealed that the NH
<jats:sub>2</jats:sub>
-termini were in the major groove nine to ten base pairs apart and were symmetrically displaced four to five base pairs from the central C of the recognition site. This result is consistent with the Y-shaped scissor grip-leucine zipper model recently proposed for a class of DNA binding proteins important in the regulation of gene expression.
</jats:p> |
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| author | Oakley, Martha G., Dervan, Peter B. |
| author_facet | Oakley, Martha G., Dervan, Peter B., Oakley, Martha G., Dervan, Peter B. |
| author_sort | oakley, martha g. |
| container_issue | 4957 |
| container_start_page | 847 |
| container_title | Science |
| container_volume | 248 |
| description | <jats:p> The NH2-terminal locations of a dimer containing the DNA binding domain of the yeast transcriptional activator GCN4 have been mapped on the binding sites 5′-CTGACTAAT-3′ and 5′-ATGACTCTT-3′. Affinity cleaving was effected by synthetic GCN4 proteins with Fe⋅EDTA moieties at the NH <jats:sub>2</jats:sub> -terminus. Analysis of the DNA cleavage patterns for dimers of the Fe⋅EDTA-proteins corresponding to GCN4 residues 222 to 281 and 226 to 281 revealed that the NH <jats:sub>2</jats:sub> -termini were in the major groove nine to ten base pairs apart and were symmetrically displaced four to five base pairs from the central C of the recognition site. This result is consistent with the Y-shaped scissor grip-leucine zipper model recently proposed for a class of DNA binding proteins important in the regulation of gene expression. </jats:p> |
| doi_str_mv | 10.1126/science.2111578 |
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| id | ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTEyNi9zY2llbmNlLjIxMTE1Nzg |
| imprint | American Association for the Advancement of Science (AAAS), 1990 |
| imprint_str_mv | American Association for the Advancement of Science (AAAS), 1990 |
| institution | DE-105, DE-14, DE-Ch1, DE-L229, DE-D275, DE-Bn3, DE-Brt1, DE-D161, DE-Gla1, DE-Zi4, DE-15, DE-Pl11, DE-Rs1 |
| issn | 0036-8075, 1095-9203 |
| issn_str_mv | 0036-8075, 1095-9203 |
| language | English |
| last_indexed | 2024-03-01T16:43:18.095Z |
| match_str | oakley1990structuralmotifofthegcn4dnabindingdomaincharacterizedbyaffinitycleaving |
| mega_collection | American Association for the Advancement of Science (AAAS) (CrossRef) |
| physical | 847-850 |
| publishDate | 1990 |
| publishDateSort | 1990 |
| publisher | American Association for the Advancement of Science (AAAS) |
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| recordtype | ai |
| series | Science |
| source_id | 49 |
| spelling | Oakley, Martha G. Dervan, Peter B. 0036-8075 1095-9203 American Association for the Advancement of Science (AAAS) Multidisciplinary http://dx.doi.org/10.1126/science.2111578 <jats:p> The NH2-terminal locations of a dimer containing the DNA binding domain of the yeast transcriptional activator GCN4 have been mapped on the binding sites 5′-CTGACTAAT-3′ and 5′-ATGACTCTT-3′. Affinity cleaving was effected by synthetic GCN4 proteins with Fe⋅EDTA moieties at the NH <jats:sub>2</jats:sub> -terminus. Analysis of the DNA cleavage patterns for dimers of the Fe⋅EDTA-proteins corresponding to GCN4 residues 222 to 281 and 226 to 281 revealed that the NH <jats:sub>2</jats:sub> -termini were in the major groove nine to ten base pairs apart and were symmetrically displaced four to five base pairs from the central C of the recognition site. This result is consistent with the Y-shaped scissor grip-leucine zipper model recently proposed for a class of DNA binding proteins important in the regulation of gene expression. </jats:p> Structural Motif of the GCN4 DNA Binding Domain Characterized by Affinity Cleaving Science |
| spellingShingle | Oakley, Martha G., Dervan, Peter B., Science, Structural Motif of the GCN4 DNA Binding Domain Characterized by Affinity Cleaving, Multidisciplinary |
| title | Structural Motif of the GCN4 DNA Binding Domain Characterized by Affinity Cleaving |
| title_full | Structural Motif of the GCN4 DNA Binding Domain Characterized by Affinity Cleaving |
| title_fullStr | Structural Motif of the GCN4 DNA Binding Domain Characterized by Affinity Cleaving |
| title_full_unstemmed | Structural Motif of the GCN4 DNA Binding Domain Characterized by Affinity Cleaving |
| title_short | Structural Motif of the GCN4 DNA Binding Domain Characterized by Affinity Cleaving |
| title_sort | structural motif of the gcn4 dna binding domain characterized by affinity cleaving |
| title_unstemmed | Structural Motif of the GCN4 DNA Binding Domain Characterized by Affinity Cleaving |
| topic | Multidisciplinary |
| url | http://dx.doi.org/10.1126/science.2111578 |