Electron microscopy of a eukaryotic single-stranded DNA binding protein-DNA complex
| Autor: | Ad Spanos, Geoffrey R. Banks, Michael V. Kairis, Ian J. Molineux |
|---|---|
| Rok vydání: | 1981 |
| Předmět: |
HMG-box
Base pair DNA polymerase DNA polymerase II DNA Single-Stranded Single-stranded binding protein Viral Proteins Structural Biology Ustilago DNA Fungal Molecular Biology Replication protein A chemistry.chemical_classification DNA ligase DNA clamp biology DNA-Binding Proteins Microscopy Electron Biochemistry chemistry DNA Viral biology.protein Nucleic Acid Conformation DNA Circular Carrier Proteins Bacteriophage phi X 174 |
| Zdroj: | Journal of Molecular Biology. 151:321-325 |
| ISSN: | 0022-2836 |
| DOI: | 10.1016/0022-2836(81)90519-2 |
| Popis: | The single-stranded DNA binding protein of Ustilago maydis decreases the contour length of φX174 DNA. When DNA complexes were prepared with subsaturating amounts of the protein, its distribution on the DNA was markedly non-random, indicating a high degree of co-operativity in its binding to single-stranded DNA. The analagous Escherichia coli, Salmonella typhimurium and bacteriophage T7 binding proteins also reduced DNA contour lengths to a similar extent, whereas the bacteriophage T4 gene 32 protein, as shown previously, increased the contour length. Despite the fact that the U. maydis protein efficiently denatures poly[d(A-T) · d(A-T)], it appears to initiate denaturation of native bacteriophage λ DNA rather inefficiently. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|