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Abstract
Previously we proved that uvsX protein catalyzes reactions similar to those thought to occur during T4 recombination (Yonesaki, T., Ryo, Y., Minagawa, T., and Takahashi, H. (1985) Eur. J. Biochem. 148, 127-134; Yonesaki, T., and Minagawa, T. (1985) EMBO J. 4, 3321-3327). Now we have found that uvsY protein stabilizes binding of uvsX protein and single-stranded DNA and weakly stimulates those reactions catalyzed by uvsX protein, although it has little activity, if any, by itself. Gene 32 protein also stimulates them weakly at low concentrations, but is strongly inhibitory at high concentrations (Yonesaki, T., and Minagawa, T. (1985) EMBO J. 4, 3321-3327; Formosa, T., and Alberts, B. M. (1986) J. Biol. Chem. 261, 6107-6118). This inhibition is counteracted by uvsY protein. The highest efficiency of uvsX protein is achieved by the co-existence of a small amount of uvsY protein and a large amount of gene 32 protein. We discuss the mechanism and the role of the three proteins in recombination.
Highlights
We have found that uvsY protein stabilizes binding of uvsX protein and single-stranded DNA and weakly stimulates those reactions catalyzed by uvsX protein, it has little activity, if any, by itself
This inhibition is counteracted by uvsY protein
We tested whether theuvsY protein would behave as a constituent of an in vitro T 4 recombination system, our previous work with the partially purified uvsY protein revealed no activity relating to DNA recombination or stimulation of uvsX function (Yonesakeit al., 1985)
Summary
1986)of bacteriophage T4, the key enzymes in this Purification of Proteins-uvsX and uvsY proteins were extracted reaction, bind to ssDNA and promote pairing between the from the respective protein-overproducing cecllosnstructedaccording ssDNA and a homologous duplex molecule. A 3.4-kilobase pair EcoRI-cleaved both key enzymes is enhanced by a class of single strand binding proteins suchas SSB protein ( M r= 18,500) of E. coli and gene 32 protein ( M , = 33,500) of T 4 phagewithin a limitedrange of the protein concentration Competent cells were co-transformed with either plasmid and pNT204 which codes for a X ts-repressor. The proteins were extracted binding of the key enzymes to ssDNA
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