Cleavage of single-stranded DNA by the A and A*proteins of bacteriophage φX174
| Autor: | J.M. de Winter, Peter Weisbeek, S.A. Langeveld, A.D.M. van Mansfeld |
|---|---|
| Rok vydání: | 1979 |
| Předmět: |
chemistry.chemical_classification
DNA ligase Deoxyribonucleases DNA clamp Base Sequence biology DNA Superhelical viruses DNA polymerase II Bacteriophage phi X174 DNA replication DNA Single-Stranded Endonucleases Primosome Molecular biology Substrate Specificity Single-stranded binding protein Molecular Weight Viral Proteins chemistry DNA Nucleotidyltransferases Genetics biology.protein Replication protein A Bacteriophage phi X 174 |
| Zdroj: | Nucleic Acids Research. 7:2177-2188 |
| ISSN: | 1362-4962 0305-1048 |
| DOI: | 10.1093/nar/7.8.2177 |
| Popis: | The purified A protein and A* protein of bacteriophage phi X174 have been tested for endonuclease activity on single stranded viral phi X174 DNA. The A protein (55.000 daltons) nicks single-stranded DNA in the same way and at the same place as it does superhelical RFI DNA, at the origin of DNA replication. The A* protein (37.000 daltons) can cleave the single-stranded viral DNA at many different sites. It has however a strong preference for the origin of replication. Both proteins generate 3'OH ends and blocked 5' termini at the nick site. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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