PURIFIED LEXA PROTEIN IS A REPRESSOR OF THE RECA AND LEXA GENES
PURIFIED LEXA PROTEIN IS A REPRESSOR OF THE RECA AND LEXA GENES
复制标题
DOI:
10.1073/pnas.78.7.4199
复制
发表时间:
1981-01-01
期刊:
影响因子:
--
通讯作者:
YANISCHPERRON, CR
中科院分区:
文献类型:
--
作者:
LITTLE, JW;MOUNT, DW;YANISCHPERRON, CR
Escherichia coli shows a pleiotropic response (the SOS response) to treatments that damage DNA or inhibit DNA replication. Apparently, the product of the lexA gene is involved in regulating the SOS response, perhaps as a repressor, and it is sensitive to the recA protease. The lexA protein is a repressor of at least 2 genes, recA and lexA. Purified protein bound specifically to the regulatory regions of the 2 genes, as judged by DNase I protection experiments, and it specifically inhibited in vitro transcription of both genes. The binding sites in recA and lexA were about 20 base pairs (bp) and 40 bp long, respectively. The 40-bp sequence in lexA was composed of 2 adjacent 20-bp sequences, which had considerable homology to one another and to the corresponding recA sequence. These 20-bp sequences, termed SOS boxes, show considerable inverted repeat structure as well. These features suggest that each box represents a single repressor binding site. Purified lexA protein was a substrate for the recA protease in a reaction requiring ATP or an analog, adenosine 5''-[.gamma.-thio]triphosphate and denatured DNA.