作者: Elisabeth DiCapua , Martine Cuillel , Elizabeth Hewat , Manfred Schnarr , Peter A. Timmins
DOI: 10.1016/0022-2836(92)90627-V
关键词: Nucleotide 、 DNA 、 Biochemistry 、 Enzyme 、 Repressor lexA 、 RNA 、 Polynucleotide 、 Cleavage (embryo) 、 Biology 、 ATP hydrolysis
摘要: Abstract RecA protein is induced by the binding of DNA and ATP to become active in hydrolysis cleavage repressors. These reactions appear depend on structural state polymerized along DNA, i.e. a helical coat six per turn 95 100 A pitch. In support this model conformation, it was shown that high concentrations salt also induce as well enzymatic activities. Here, we describe that, vitro with non-hydrolyzable analogue ATPγS, RNA heparin can both transition activation LexA accordance model. do not reaction presence ATP, they either, suggesting contrast nucleotide bound stably enough, combined affinities polynucleotide actually modulate discrimination for various possible inducers vivo .