HMG protein binding to an A/T-rich positive regulatory region of the pea plastocyanin gene promoter
| Autor: | Keng-Hock Pwee, John C. Gray, Carl I. Webster |
|---|---|
| Rok vydání: | 1994 |
| Předmět: |
DNA
Plant Molecular Sequence Data Plant Science Biology Genes Plant DNA-binding protein chemistry.chemical_compound Genetics Deoxyribonuclease I Plastocyanin Promoter Regions Genetic Gene Cell Nucleus Base Composition Base Sequence DNase-I Footprinting High Mobility Group Proteins Peas Promoter General Medicine Hmg protein Proteinase K Molecular biology DNA-Binding Proteins Biochemistry chemistry biology.protein Agronomy and Crop Science DNA Protein Binding Subcellular Fractions |
| Zdroj: | Plant Molecular Biology. 26:1907-1920 |
| ISSN: | 1573-5028 0167-4412 |
| DOI: | 10.1007/bf00019502 |
| Popis: | Gel retardation assays using pea nuclear extracts have detected specific binding to regions of the promoter of the pea plastocyanin gene (petE). Several complexes which differ in sensitivity to competition with unlabelled promoter fragments and various DNA alternating copolymers, to heat treatment and to digestion with proteinase K have been detected. A protein factor, PCF1, forming one of these complexes was heat-stable and most sensitive to competition with poly(dAdT).poly(dAdT) compared to other alternating copolymers. DNase I footprinting assays showed that tracts of A/T-rich sequence within the -444 to -177 positive regulatory region of the petE promoter were protected in the presence of the pea nuclear extract. The factor PCF1 copurified with a high-mobility-group (HMG) protein preparation from pea chromatin. DNase I footprinting with the HMG protein preparation demonstrated that similar tracts of A/T-rich sequences within the promoter were protected. Southwestern-blot analysis of pea HMG proteins purified by gel filtration through Superose 12 detected a single DNA-binding species of 21 kDa. The properties of the factor PCF1 suggest that it is likely to be an HMG I protein. |
| Databáze: | OpenAIRE |
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