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Correlated cleavage of single‐ and double‐stranded substrates by uracil‐DNA glycosylase
Author(s) -
Sidorenko Viktoriya S.,
Mechetin Grigory V.,
Nevinsky Georgy A.,
Zharkov Dmitry O.
Publication year - 2008
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/j.febslet.2008.01.002
Subject(s) - uracil dna glycosylase , dna glycosylase , uracil , cleavage (geology) , chemistry , dna , biochemistry , biophysics , biology , dna repair , paleontology , fracture (geology)
Uracil‐DNA glycosylase (Ung) can quickly locate uracil bases in an excess of undamaged DNA. DNA glycosylases may use diffusion along DNA to facilitate lesion search, resulting in processivity, the ability of glycosylases to excise closely spaced lesions without dissociating from DNA. We propose a new assay for correlated cleavage and analyze the processivity of Ung. Ung conducted correlated cleavage on double‐ and single‐stranded substrates; the correlation declined with increasing salt concentration. Proteins in cell extracts also decreased Ung processivity. The correlated cleavage was reduced by nicks in DNA, suggesting the intact phosphodiester backbone is important for Ung processivity.