Cleavage and sequence recognition of 2,6-diaminopurine-containing DNA by site-specific endonucleases.
The susceptibility of 2,6-diaminopurine (DAP)-containing bacteriophage DNA to several restriction and other endonucleases was examined. With the only exception of TaqI, these enzymes did not accept the modified base as a substitute for adenine. The phage DNA was extensively fragmented by the restriction endonucleases which recognize only G and C-containing sites. 5'-terminal analysis of the MspI and SmaI fragments revealed that d(DAP-T) basepairs can be mistaken by some enzymes for d(G-C) pairs.
Szekeres
M
M
Institute of Plant Physiology, Biological Research Center, Szeged, Hungary.
Matveyev
A V
AV
D015075:2-Aminopurine / Q000031:analogs & derivatives*; D000225:Adenine / Q000031:analogs & derivatives*; D001483:Base Sequence; D004262:DNA Restriction Enzymes / Q000378:metabolism*; D004279:DNA, Viral; D007700:Kinetics; D013379:Substrate Specificity
D004279:DNA, Viral; D015075:2-Aminopurine; C007300:2,6-diaminopurine; D004262:DNA Restriction Enzymes; D000225:Adenine