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• W2034286246 abstract "Elaine B. Newman,’ Richard D’Ari,t and Rong Tuan Lin’ *Biology Department Concordia University Montreal, Quebec H3G lM8 Canada tlnstrtut Jacques Monod Centre National de la Recherche Scientifique Universite Paris 7 75251 Paris Cedex 05 France The concept of the regulon arose from studies showing that a single transcriptional regulator can control several distinct operons. The first regulons discovered were simi- lar to operons in that the member functions were involved in a specific physiological role, such as the uptake and utilization of maltose. The idea was generalized with the recognition of global responses, in which a number of func- tions are coordinately controlled in response to an environ- mental signal (e.g., temperature or pH). The factor mediat- ing transcriptional regulation in a global response can be a transcriptional repressor (LexA), a transcriptional activator (PhoB), a combined repressor-activator (Crp), an alterna- tive sigma factor (RpoH, NtrA), or an RNA polymerase effector (ppGpp). The sets of physiologically related functions that are grouped together in most global responses tend to reflect questions experimenters ask: How does the cell respond to starvation? How does the cell react to DNA damage? The leucine-Lrp regulon was discovered in aslightlydiffer- ent way. The leucine-responsive regulatory protein, Lrp, which governs expression of the leucine-Lrp regulon (Platko et al., 1990), was independently identified several times as a regulator of various members of the regulon (see table: Anderson et al., 1976; Andrews et al., 1986; Riccaetal., 1989; Linet al., 1990). Operonsofthe leucine- Lrp regulon can be controlled either positively or nega- tively, as in the Crp-CAMP regulon. Leucine is clearly a major effector of the regulon, in that it affects Lrp regulation in many, but not all, cases. However, we do not yet know what aspect of the environment leucine represents. This sets the leucine-Lrp regulon apart-a global response in search of a physiological rationale. The difference, how- ever, is probably more methodological than real. Lrp is a 19 kd DNA-binding protein, existing in solution as a dimer (Willins et al., 1991). Apart from its lack of tryptophan residues, Lrp has no unusual structural fea- tures compared with other DNA-binding proteins. The only E. coli DNA-binding protein with which it has sequence similarity is AsnC, activator of the asnA gene. In particular," @default.
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• W2034286246 date "1992-02-01" @default.
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• W2034286246 title "The leucine-Lrp regulon in E. coli: A global response in search of a raison d'Être" @default.
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• W2034286246 doi "https://doi.org/10.1016/0092-8674(92)90135-y" @default.
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