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Single‐stranded DNA binding protein and DNA helicase of bacteriophage T7 mediate homologous DNA strand exchange.
Author(s) -
Kong D.,
Richardson C. C.
Publication year - 1996
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1996.tb00552.x
Subject(s) - biology , dna , dna clamp , single stranded binding protein , helicase , microbiology and biotechnology , primase , replication protein a , dna binding protein , bacteriophage , circular bacterial chromosome , homologous chromosome , dna polymerase ii , genetics , dna replication , gene , escherichia coli , transcription factor , polymerase chain reaction , rna , reverse transcriptase
Two proteins encoded by bacteriophage T7, the gene 2.5 single‐stranded DNA binding protein and the gene 4 helicase, mediate homologous DNA strand exchange. Gene 2.5 protein stimulates homologous base pairing of two DNA molecules containing complementary single‐stranded regions. The formation of a joint molecule consisting of circular, single‐stranded M13 DNA, annealed to homologous linear, duplex DNA having 3′‐ or 5′‐single‐stranded termini of approximately 100 nucleotides requires stoichiometric amounts of gene 2.5 protein. In the presence of gene 4 helicase, strand transfer proceeds at a rate of > 120 nucleotides/s in a polar 5′ to 3′ direction with respect to the invading strand, resulting in the production of circular duplex M13 DNA. Strand transfer is coupled to the hydrolysis of a nucleoside 5′‐triphosphate. The reaction is dependent on specific interactions between gene 2.5 protein and gene 4 protein.