Premium
Cleavage and sequence recognition of 2,6‐diaminopurine‐containing DNA by site‐specific endonucleases
Author(s) -
Szekeres Miklós,
Matveyev Andrey V.
Publication year - 1987
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(87)80197-7
Subject(s) - cleavage (geology) , dna , recognition sequence , sequence (biology) , chemistry , stereochemistry , computational biology , restriction enzyme , genetics , biology , biochemistry , paleontology , fracture (geology)
The susceptibility of 2,6‐diaminopurine (DAP)‐containing bacteriophage DNA to several restriction and other endonucleases was examined. With the only exception of Taq I, 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 Msp I and Sma I fragments revealed that d(DAP‐T) basepairs can be mistaken by some enzymes for d(G‐C) pairs.