TY - JOUR
T1 - The interaction of T4 endonuclease V E23Q mutant with thymine dimer- and tetrahydrofuran-containing DNA
AU - Latham, K. A.
AU - Manuel, R. C.
AU - Lloyd, R. S.
PY - 1995
Y1 - 1995
N2 - The interaction between endonuclease V, the cyclobutane pyrimidine dimer- specific N-glycosylase/abasic lyase from bacteriophage T4, and DNA was investigated by DNase I footprinting methods. The catalytically inactive mutant E23Q was found to interact with a smaller region of DNA at the abasic site analog, tetrahydrofuran, than at a thymine dimer site. Like the wild- type enzyme, the mutant contacted the DNA substrates primarily on the strand opposite the damage. The various complexes examined by footprinting techniques represent distinct points along the catalytic pathway of endonuclease V: before catalysis at a dimer, after N-glycosylase action but before abasic lyase action, and before catalysis at an abasic site. The differences between the footprints of the mutant and wild-type enzymes on both DNA substrates likely represent subtly different conformations within these complexes.
AB - The interaction between endonuclease V, the cyclobutane pyrimidine dimer- specific N-glycosylase/abasic lyase from bacteriophage T4, and DNA was investigated by DNase I footprinting methods. The catalytically inactive mutant E23Q was found to interact with a smaller region of DNA at the abasic site analog, tetrahydrofuran, than at a thymine dimer site. Like the wild- type enzyme, the mutant contacted the DNA substrates primarily on the strand opposite the damage. The various complexes examined by footprinting techniques represent distinct points along the catalytic pathway of endonuclease V: before catalysis at a dimer, after N-glycosylase action but before abasic lyase action, and before catalysis at an abasic site. The differences between the footprints of the mutant and wild-type enzymes on both DNA substrates likely represent subtly different conformations within these complexes.
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U2 - 10.1128/jb.177.17.5166-5168.1995
DO - 10.1128/jb.177.17.5166-5168.1995
M3 - Article
C2 - 7665500
AN - SCOPUS:0029127485
SN - 0021-9193
VL - 177
SP - 5166
EP - 5168
JO - Journal of bacteriology
JF - Journal of bacteriology
IS - 17
ER -