Mechanism of cos DNA cleavage by bacteriophage λ terminase: Multiple roles of ATP
- 1 September 1988
- Vol. 54 (6) , 765-775
- https://doi.org/10.1016/s0092-8674(88)91021-5
Abstract
No abstract availableThis publication has 46 references indexed in Scilit:
- Prediction of an ATP reactive center in the small subunit, gpNu1, of the phage lambda terminase enzymeJournal of Molecular Biology, 1988
- Prohead and DNA-gp3-dependent ATPase activity of the DNA packaging protein gp16 of bacteriophage φ29Journal of Molecular Biology, 1987
- Cutting of chi-like sequences by the RecBCD enzyme of Escherichia coliJournal of Molecular Biology, 1987
- Isolation of intermediates in the binding of the FLP recombinase of the yeast plasmid 2-micron circle to its target sequenceJournal of Molecular Biology, 1987
- Terminase and the recognition, cutting and packaging of λ chromosomesTrends in Genetics, 1986
- Lambda phage protein Nu 1 contains the conserved DNA binding fold of repressorsJournal of Molecular Biology, 1986
- Substrate specificity of the DNA unwinding activity of the RecBC enzyme of Escherichia coliJournal of Molecular Biology, 1985
- The terminase of bacteriophage λJournal of Molecular Biology, 1985
- A functional domain of bacteriophage λ terminase for prohead bindingJournal of Molecular Biology, 1984
- Knotting of DNA caused by a genetic rearrangementJournal of Molecular Biology, 1983