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In Vivo role of Site‐Directed Cleavage of DNA by the RecA‐dependent nuclease Ref
Author(s) -
Baker Staci J.,
Ronayne Erin A.,
Cox Michael M.
Publication year - 2013
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.27.1_supplement.760.3
Subject(s) - nuclease , cleave , dna , bacteriophage , duplex (building) , cleavage (geology) , chemistry , oligonucleotide , homologous recombination , microbiology and biotechnology , biology , gene , escherichia coli , biochemistry , paleontology , fracture (geology)
The Ref protein, encoded by bacteriophage P1, is a RecA‐dependent nuclease. A member of the HNH nuclease family, Ref will cleave DNA only if it is bound by the RecA protein. When RecA filaments are formed on an oligonucleotide and used to form a D‐loop in a target duplex DNA, Ref will cleave both strands of the target DNA within the D‐loop. In this mode of action, Ref is effectively a universal restriction enzyme. The function of Ref nuclease in the life cycle of bacteriophage P1 and related bacteriophages is a mystery. In this report, we will present data related to the in vivo function of Ref. In particular, wild type Ref protein both enhances certain types of RecA‐dependent recombination events and also suppresses P1 lysogenation.