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High affinity interaction of mammalian DNA topoisomerase I with short single‐ and double‐stranded oligonucleotides
Author(s) -
Nevinsky Georgy A.,
Bugreev Dmitry V.,
Buneva Valenti.,
Yasui Yoshihiro,
Nishizawa Miwako,
Andoh Toshiwo
Publication year - 1995
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(95)00609-d
Subject(s) - oligonucleotide , topoisomerase , dna , chemistry , biophysics , double stranded , microbiology and biotechnology , biochemistry , computational biology , biology
The interaction of DNA topoisomerase I (topo I) with a set of single‐ and double‐stranded oligonucleotides containing 5–27 mononucleotides was investigated. All single‐ and double‐stranded oligonucleotides were found to inhibit competitively the supercoiled DNA relaxation reaction catalyzed by topo I. The enzyme affinity for specific sequence pentanucleotides of the scissile (GACTT, K i = 2 μ M) and non‐cleaved chain (AAGTC, K i = 110 μ M) is about 2–4 orders of magnitude higher than that for non‐specific oligonucleotides. This specific sequence affinity increases in several cases: lengthening of single‐stranded oligonucleotides, formation of stable duplexes between complementary oligonucleotides and preincubation of the enzyme with ligands before addition of supercoiled DNA. We assume that oligonucleotides having a high affinity to the enzyme can offer a unique opportunity for rational design of topoisomerase‐targeting drugs.