Abstract
E. coli RecA protein promotes homologous pairing and reciprocal strand exchange reactions between duplex DNA molecules in vitro. Reaction intermediates contain Holliday junctions that are driven along the DNA at a maximal rate approaching 1000 bases per minute. T4 endonuclease VII cleaves Holliday junctions in vitro, and its inclusion in RecA-mediated reactions leads to the rapid formation of heteroduplex products. Product analysis indicates patch and splice recombinant molecules similar to those expected from in vivo recombination events. The combined formation and resolution of Holliday junctions has led us to propose a model for resolution based on the structure of RecA-DNA helices. One feature of this model is that resolution, which gives rise to the two types of recombinant product, may occur without need for isomerization of the junction.
| Original language | English |
|---|---|
| Pages (from-to) | 329-336 |
| Number of pages | 8 |
| Journal | Cell |
| Volume | 60 |
| Issue number | 2 |
| DOIs | |
| Publication status | Published - 26 Jan 1990 |
Keywords
- Bacteriophage phi X 174
- Base Sequence
- DNA, Circular
- DNA, Viral
- Endodeoxyribonucleases
- Escherichia coli
- Models, Structural
- Molecular Sequence Data
- Nucleic Acid Conformation
- Nucleic Acid Heteroduplexes
- Protein Conformation
- Rec A Recombinases
- Restriction Mapping
- T-Phages