Radioprotection of DNA by a DNA-binding Protein: MC1 Chromosomal Protein from the ArchaebacteriumMethanosarcinasp.CHTI55
| Autor: | Melanie Spotheim-Maurizot, B. Laine, J. Franchet-Beuzit, Michel Charlier, R. Sabattier, V. Isabelle |
|---|---|
| Rok vydání: | 1993 |
| Předmět: |
DNA
Bacterial Base pair Archaeal Proteins Molecular Sequence Data Radiation-Protective Agents Biology Fast Neutrons chemistry.chemical_compound Plasmid Bacterial Proteins Radiology Nuclear Medicine and imaging A-DNA Amino Acid Sequence Gel electrophoresis Base Sequence Radiological and Ultrasound Technology Binding protein Chromosome Archaea Molecular biology PBR322 DNA-Binding Proteins Ribonucleoproteins Biochemistry chemistry DNA |
| Zdroj: | International Journal of Radiation Biology. 63:749-758 |
| ISSN: | 1362-3095 0955-3002 |
| Popis: | The archaebacterial chromosomal protein MC1 binds tightly and unspecifically to DNA; binding protects DNA against radiolysis by fast neutrons. At low covering of pBR322 plasmid DNA, one bound protein protects some 50 attack sites (phosphate-sugar moieties) against both single (ssb) and double strand breaks (dsb). At high covering of plasmid, protection against dsb becomes almost complete, although about half of the attack sites remain accessible to ssb. DNA restriction fragments were used to investigate the organization of the complexes, and its consequences on DNA radiolysis. Sequencing gel electrophoresis of the radiolytically-broken fragments are almost regular in the absence of protein, showing that breakage occurs at every base. In the presence of the protein, a periodic protection pattern is observed. The period of 11 base pairs is interpreted as the minimum distance between two adjacent MC1 proteins. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|