E. coli recA protein possesses a strand separating activity on short duplex DNAs
| Autor: | Marco Bianchi, B Riboli, G. E. Magni |
|---|---|
| Rok vydání: | 1985 |
| Předmět: |
DNA clamp
General Immunology and Microbiology General Neuroscience Circular bacterial chromosome Nucleic Acid Heteroduplexes DNA Biology General Biochemistry Genetics and Molecular Biology Rec A Recombinases Structure-Activity Relationship chemistry.chemical_compound D-loop Heavy strand chemistry Biochemistry Coding strand Escherichia coli Biophysics DNA supercoil Electrophoresis Polyacrylamide Gel Molecular Biology Research Article Plasmids Transcription bubble |
| Zdroj: | The EMBO Journal. 4:3025-3030 |
| ISSN: | 0261-4189 |
| DOI: | 10.1002/j.1460-2075.1985.tb04039.x |
| Popis: | RecA protein was found to catalyze the dissociation of the strands of a DNA substrate consisting of a 20-nucleotide primer annealed to circular single-stranded M13mp DNA. The strand separation reaction requires ATP hydrolysis and the presence of single-stranded DNA flanking the duplex DNA region to be unwound. RecA-catalyzed strand separation is effective only for very short duplexes, not exceeding 30 bp, and is not stimulated by single-stranded DNA-binding protein. These results are consistent with the ability of recA protein to disrupt regions of secondary structure in single-stranded DNA and to incorporate large non-homologies into heteroduplex DNA. |
| Databáze: | OpenAIRE |
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