AraC protein, regulation of the l-arabinose operon in Escherichia coli, and the light switch mechanism of AraC action

被引:195
作者
Schleif, Robert [1 ]
机构
[1] Johns Hopkins Univ, Dept Biol, Baltimore, MD 21218 USA
关键词
allostery; transcription initiation; RNA polymerase; solubility; fluorescence; homology; fucose; DNA-BINDING DOMAIN; TRANSCRIPTION START SITE; AMP RECEPTOR PROTEIN; AMINO-ACID CONTACTS; GEL-ELECTROPHORESIS; BETA-GALACTOSIDASE; INDUCTION KINETICS; CRYSTAL-STRUCTURE; LAC REPRESSOR; IN-VIVO;
D O I
10.1111/j.1574-6976.2010.00226.x
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
This review covers the physiological aspects of regulation of the arabinose operon in Escherichia coli and the physical and regulatory properties of the operon's controlling gene, araC. It also describes the light switch mechanism as an explanation for many of the protein's properties. Although many thousands of homologs of AraC exist and regulate many diverse operons in response to many different inducers or physiological states, homologs that regulate arabinose-catabolizing genes in response to arabinose were identified. The sequence similarities among them are discussed in light of the known structure of the dimerization and DNA-binding domains of AraC.
引用
收藏
页码:779 / 796
页数:18
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