Importance of minor groove binding zinc fingers within the transcription factor IIIA-DNA complex
| Autor: | Laura Neely, John W. Trauger, Peter B. Dervan, Eldon E. Baird, Joel M. Gottesfeld |
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| Rok vydání: | 1997 |
| Předmět: |
Guanine
Protein Conformation Biology DNA-binding protein law.invention chemistry.chemical_compound Structural Biology law Transcription Factor TFIIIA Deoxyribonuclease I Binding site Molecular Biology Transcription factor Zinc finger Binding Sites Zinc Fingers DNA Zinc finger nuclease Recombinant Proteins DNA-Binding Proteins Nylons Biochemistry chemistry Recombinant DNA Groove (joinery) Transcription Factors |
| Zdroj: | Journal of Molecular Biology. 274:439-445 |
| ISSN: | 0022-2836 |
| DOI: | 10.1006/jmbi.1997.1411 |
| Popis: | The gene-specific transcription factor IIIA (TFIIIA) binds to the internal promoter element of the 5 S rRNA gene through nine zinc fingers which make specific DNA contacts. Seven of the nine TFIIIA zinc fingers participate in major groove DNA contacts while two fingers, 4 and 6, have been proposed to bind in or across the minor groove. Pyrrole-imidazole polyamides are minor groove binding ligands that recognize predetermined DNA sequences with affinity and specificity comparable to natural DNA-binding proteins. We have examined the DNA binding activity of nine finger TFIIIA and shorter recombinant analogs in the presence of polyamides that bind six base-pair sequences (K_d = 0.03 to 1.7 nM) in the minor groove of the binding site for zinc finger 4. DNase I footprint titrations demonstrate that the polyamides and a recombinant protein containing the three amino-terminal zinc fingers of TFIIIA (zf1-3) co-occupy the TFIIIA binding site, in agreement with the known location of zf1-3 in the major groove. In contrast, the polyamides block the specific interaction of TFIIIA or zf1-4 with the 5 S RNA gene, supporting a model for minor groove occupancy by zinc finger 4. Minor groove binding polyamides targeted to specific DNA sequences may provide a novel chemical approach to probing multidomain protein-DNA interactions. |
| Databáze: | OpenAIRE |
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