RecA蛋白与经N-羟基-2-乙酰氨基芴和4-羟基氨基喹啉1-氧化物修饰的pBR322 DNA的相互作用。

Interaction of RecA protein with pBR322 DNA modified by N-hydroxy-2-acetylaminofluorene and 4-hydroxyaminoquinoline 1-oxide.

作者信息

Kojima M, Suzuki M, Morita T, Ogawa T, Ogawa H, Tada M

机构信息

Laboratory of Biochemistry, Aichi Cancer Center Research Institute, Nagoya, Japan.

出版信息

Nucleic Acids Res. 1990 May 11;18(9):2707-14. doi: 10.1093/nar/18.9.2707.

DOI:10.1093/nar/18.9.2707

PMID:2140154

原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC330755/

Abstract

Interaction of RecA protein of Escherichia coli with pBR322 DNA modified by N-hydroxy-2-acetylaminofluorene (N-OH-AAF) and 4-hydroxyaminoquinoline 1-oxide (4HAQO) was investigated. RecA protein bound more efficiently to modified DNA than to unmodified DNA as judged by filter-binding and gel electrophoresis assay. The binding of RecA protein with modified DNA resulted in the stimulation of ATPase activity and the activation for RecA protein to stimulate the repressor cleavage. These abilities of RecA protein were increased proportionally to the number of adducts in the plasmid DNA (0-5 adducts). Apurinic and alkylated DNA did not activate RecA protein. We suggest that modification of DNA by N-OH-AAF and 4HAQO provides binding sites for RecA protein and may act as an activation signal for SOS response.

摘要

研究了大肠杆菌RecA蛋白与经N-羟基-2-乙酰氨基芴（N-OH-AAF）和4-羟基氨基喹啉1-氧化物（4HAQO）修饰的pBR322 DNA的相互作用。通过滤膜结合和凝胶电泳分析判断，RecA蛋白与修饰DNA的结合比与未修饰DNA的结合更有效。RecA蛋白与修饰DNA的结合导致ATP酶活性的刺激以及RecA蛋白刺激阻遏物切割的激活。RecA蛋白的这些能力与质粒DNA中加合物的数量（0-5个加合物）成比例增加。脱嘌呤和烷基化的DNA不激活RecA蛋白。我们认为，N-OH-AAF和4HAQO对DNA的修饰为RecA蛋白提供了结合位点，并可能作为SOS反应的激活信号。