Regulation of SOS functions: Purification of E. coli LexA protein and determination of its specific site cleaved by the RecA protein
作者： Toshihiro Horii , Tomoko Ogawa , Tomoyuki Nakatani , Toshiharu Hase , Hiroshi Matsubara
DOI: 10.1016/0092-8674(81)90393-7
关键词:
摘要: The LexA protein of Escherichia coli was purified to more than 96% purity from cells harboring a recombinant plasmid carrying the lexA gene with lacZ promoter sequence. amino acid composition and its amino-terminal sequence were analyzed. results are in agreement prediction nucleotide gene. is cleaved into two polypeptides by E. RecA presence ATP single-stranded DNA. site specific cleavage determined analyzing sequences products at carboxyl termini. found occur single between Ala84 Gly85.
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