Open AccessThe old exonuclease of bacteriophage P2
Author(s) -
Heejoon Myung,
Richard Calendar
Publication year - 1995
Publication title -
journal of bacteriology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.652
H-Index - 246
eISSN - 1067-8832
pISSN - 0021-9193
DOI - 10.1128/jb.177.3.497-501.1995
Subject(s) - nuclease , exonuclease , biology , recbcd , dna , bacteriophage , biochemistry , microbiology and biotechnology , escherichia coli , maltose binding protein , exonuclease iii , dna polymerase , dna repair , gene , recombinant dna , fusion protein
The Old protein of bacteriophage P2 is responsible for interference with the growth of phage lambda and for killing of recBC mutant Escherichia coli. We have purified Old fused to the maltose-binding protein to 95% purity and characterized its enzymatic properties. The Old protein fused to maltose-binding protein has exonuclease activity on double-stranded DNA as well as nuclease activity on single-stranded DNA and RNA. The direction of digestion of double-stranded DNA is from 5' to 3', and digestion initiates at either the 5'-phosphoryl or 5'-hydroxyl terminus. The nuclease is active on nicked circular DNA, degrades DNA in a processive manner, and releases 5'-phosphoryl mononucleotides.