HMG proteins (1+2) form beaded structures when complexed with closed circulac DNA
| Autor: | Diane Mathis, A. Kindelis, Corrado Spadafora |
|---|---|
| Rok vydání: | 1980 |
| Předmět: |
Chromosomal Proteins
Non-Histone Macromolecular Substances Simian virus 40 Thymus Gland Plasma protein binding Mitochondrion Histones chemistry.chemical_compound Genetics Animals Nucleosome Nuclease biology High Mobility Group Proteins Hmg protein Nucleosomes Microscopy Electron Histone High-mobility group Biochemistry chemistry DNA Viral biology.protein Cattle DNA Circular DNA Protein Binding |
| Zdroj: | Nucleic Acids Research. 8:2577-2590 |
| ISSN: | 1362-4962 0305-1048 |
| DOI: | 10.1093/nar/8.12.2577 |
| Popis: | Structures bearing a resemblance to nucleosomes can be assembled by incubating calf thymus High Mobility Group proteins (1 + 2) with closed circular DNA. These HMG proteins are capable of forming beads and inducing superhelicity when bound to DNA. However, they do not protect from nuclease digestion the discrete DNA fragments characteristic of nucleosomes. The relationship between HMGs (1 + 2) and the "primitive" histone-like DNA-packaging proteins from prokaryotes and mitochondria is discussed. |
| Databáze: | OpenAIRE |
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