[Structure of the interaction sites of eukaryotic DNA with steroid hormone-apolipoprotein A-I complexes].
A high affinity of apolipoprotein A-I for DNA and synthetic oligonucleotides was found using the affinity chromatography, affinity modification, and enzyme analysis. The competitive inhibition and Southern hybridization allowed disclosing the specificity of the interaction of the tetrahydrocortisol-apolipoprotein A-I complex (THC-ApoA-I) with high molecular weight DNA in regions contained GCC/CGG-sequences. The S1 nuclease sensitivity of the duplex CC(GCC)3 x GG(CGG)3 was found to occur under the action of THC-ApoA-I complex. The role of the interaction sites of eukaryotic DNA with steroid (THC, androsterone)-ApoA-I complexes in the initiation of the copy reaction in vitro was revealed.
Panin
L E
LE
Gimautdinova
O I
OI
Kuznetsov
P A
PA
Velichko
E Iu
EIu
Bazaluk
V V
VV
D000818:Animals; D016632:Apolipoprotein A-I / Q000737:chemistry*; D001483:Base Sequence; D001665:Binding Sites; D015139:Blotting, Southern; D002846:Chromatography, Affinity; D004247:DNA / Q000737:chemistry*; D009690:Nucleic Acid Conformation; D009841:Oligonucleotides / Q000737:chemistry; D051381:Rats; D015719:Single-Strand Specific DNA and RNA Endonucleases / Q000737:chemistry; D013256:Steroids / Q000737:chemistry; D013760:Tetrahydrocortisol / Q000737:chemistry*
D016632:Apolipoprotein A-I; D009841:Oligonucleotides; D013256:Steroids; D013760:Tetrahydrocortisol; D004247:DNA; D015719:Single-Strand Specific DNA and RNA Endonucleases