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J. Biol. Chem., Vol. 268, Issue 32, 23830-23836, Nov, 1993
R Hanai and JC Wang
We have examined the biological role and catalytic function of two
juxtaposed tyrosyl residues in the bacteriophage phi X174 gene A protein,
Tyr-343 and Tyr-347, which have been implicated in the catalysis of
sequence-specific DNA strand transfer. Site-directed mutagenesis changing
either tyrosine to phenylalanine abolishes phage viability. The biochemical
basis of this inviability was studied using purified A* protein containing
the carboxyl-terminal 341 amino acids of the A protein, as well as purified
A* protein with a Y343F or Y347F mutation. All three proteins can cleave
the phi X174 replication origin and perform strand transfer between
oligodeoxynucleotides bearing the recognition sequence of the A protein;
however, both Tyr-343 and Tyr- 347 appear to be required for coordinated
DNA strand transfer by a single A* protein molecule. The chirality of a
phosphorothioate group at the site of strand transfer in the DNA was found
to be retained following the strand-transfer reaction, which argues against
transfer of Tyr-343-linked DNA to Tyr-347 on the same protein molecule or
vice versa. These results support the current model of gene A protein
function in which the two tyrosines of a single protein molecule alternate
in catalyzing DNA strand transfer at the viral replication origin.
The mechanism of sequence-specific DNA cleavage and strand transfer by phi X174 gene A* protein
Department of Biochemistry and Molecular Biology, Harvard University, Cambridge, Massachusetts 02138.
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