The Interaction of the A and A* Proteins of Bacteriophage φX174 with Single-Stranded and Double-Stranded φX DNA in vitro
| Autor: | S.A. Langeveld, Arie van der Ende, Peter Weisbeek, Gerard A. van Arkel |
|---|---|
| Rok vydání: | 2005 |
| Předmět: |
Recombination
Genetic chemistry.chemical_classification biology genetic processes Bacteriophage phi X174 DNA Single-Stranded Sequence (biology) Plasma protein binding biology.organism_classification Biochemistry Divalent Bacteriophage Microscopy Electron Viral Proteins enzymes and coenzymes (carbohydrates) chemistry.chemical_compound Crystallography chemistry DNA Viral health occupations Molecule Centrifugation Bacteriophage phi X 174 DNA Protein Binding |
| Zdroj: | European Journal of Biochemistry. 124:245-252 |
| ISSN: | 1432-1033 0014-2956 |
| DOI: | 10.1111/j.1432-1033.1982.tb06584.x |
| Popis: | The binding of the bacteriophage phi X 174-coded A and A* proteins to single-stranded (ssDNA) and double-stranded (dsDNA ) phi X DNA was studied by electron microscopy. The interaction of the A* protein with ssDNA and dsDNA was also studied by sedimentation velocity centrifugation. It was shown that the binding of the A and A* proteins to ssDNA occurs in a non-cooperative manner and requires no or very little sequence specificity under the conditions used here. Both protein-ssDNA complexes have the same compact structure caused by intrastrand cross-linking through the interaction of protein molecules with separate parts of the ssDNA molecule. The A protein does not bind to phi X dsDNA in the absence of divalent cations. The A* protein does bind to dsDNA, although it has a strong preference for binding to ssDNA. The structure of the A* protein-dsDNA complexes is different from that of the A* protein-ssDNA complexes, as the former have a rosette-like structure caused by protein-protein interactions. High ionic strengths favour the formation of large condensed aggregates. |
| Databáze: | OpenAIRE |
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