• Katsushi Yokoyama, Sanae A Ishijima, Lester Clowney, Hideaki Koike, Hironori Aramaki, Chikako Tanaka, Kozo Makino, and Masashi Suzuki.
• National Institute of Advanced Industrial Science and Technology, AIST Tsukuba Center, Tsukuba, Japan.
• FEMS Microbiol. Rev. 2006 Jan 1; 30 (1): 89-108.

AbstractFeast/famine regulatory proteins comprise a diverse family of transcription factors, which have been referred to in various individual identifications, including Escherichia coli leucine-responsive regulatory protein and asparagine synthase C gene product. A full length feast/famine regulatory protein consists of the N-terminal DNA-binding domain and the C-domain, which is involved in dimerization and further assembly, thereby producing, for example, a disc or a chromatin-like cylinder. Various ligands of the size of amino acids bind at the interface between feast/famine regulatory protein dimers, thereby altering their assembly forms. Also, the combination of feast/famine regulatory protein subunits forming the same assembly is altered. In this way, a small number of feast/famine regulatory proteins are able to regulate a large number of genes in response to various environmental changes. Because feast/famine regulatory proteins are shared by archaea and eubacteria, the genome-wide regulation by feast/famine regulatory proteins is traceable back to their common ancestor, being the prototype of highly differentiated transcription regulatory mechanisms found in organisms nowadays.

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