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Papers In Press, published online ahead of print December 20, 2002
J. Biol. Chem, 10.1074/jbc.M210605200
Submitted on October 16, 2002
Revised on December 19, 2002
Accepted on December 19, 2002

The DNA binding domain of the gene 2.5 single-stranded DNA binding protein of bacteriophage T7

Edel M. Hyland, Lisa F. Rezende, and Charles C. Richardson

Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115

Corresponding Author: ccr{at}hms.harvard.edu

Gene 2.5 of bacteriophage T7 encodes a single-stranded DNA binding protein that is essential for viral survival. Its crystal structure reveals a conserved oligosaccharide/oligonucleotide binding fold predicted to interact with single-stranded DNA. However, there was to experimental evidence to support this hypothesis. Recently, we reported a genetic for lethal mutations in gene 2.5 that we are using to identify functional domains of the gene 2.5 protein. This screen uncovered a number of mutations that led to amino acid substitutions in the proposed DNA binding domain. Three variant proteins, gp2.5-Y158C, gp2.5-K152E and gp2.5-Y111C/Y158C, exhibit a decrease in binding affinity for oligonucleotides. A fourth, gp2.5-K109I, exhibits an altered mode of binding single-stranded DNA. A carboxyl-terminal truncation of gene 2.5 protein, gp 2.5-?26C, binds single-stranded DNA ten-fold more tightly than the wild-type protein. The three altered proteins defective in single-stranded DNA binding cannot mediate the annealing of homologous DNA, whereas gp2.5-?26C mediates the reaction more effectively than does wild-type. Gp2.5 -K109I retains this annealing ability, albeit slightly less efficiently. With the exception of gp2.5-?26C, all variant proteins form dimers in solution and physically interact with T7 DNA polymerase.


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