The old exonuclease of bacteriophage P2.
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.
Myung
H
H
Department of Molecular and Cell Biology, University of California, Berkeley.
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D000251:Adenosine Triphosphatases / Q000378:metabolism; D017901:Bacteriophage P2 / Q000201:enzymology*; D001483:Base Sequence; D004247:DNA / Q000378:metabolism; D003851:Deoxyribonucleases / Q000494:pharmacology; D005092:Exonucleases / Q000302:isolation & purification*; D008969:Molecular Sequence Data; D013379:Substrate Specificity; D014764:Viral Proteins / Q000302:isolation & purification*
C079414:Old protein, Enterobacteria phage P2; D014764:Viral Proteins; D004247:DNA; D003851:Deoxyribonucleases; D005092:Exonucleases; D000251:Adenosine Triphosphatases