STRUCTURAL CONSERVATION IN THE CHEY SUPERFAMILY
STRUCTURAL CONSERVATION IN THE CHEY SUPERFAMILY
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DOI:
10.1021/bi00095a001
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发表时间:
1993-11-09
期刊:
影响因子:
2.9
通讯作者:
VOLZ, K
中科院分区:
文献类型:
--
作者:
VOLZ, K
Bacteria adaptively respond to a wide varietyof stimuli encountered in their unpredictableenvironment. Their be-havioral responses enable establishment and maintainance of infectious states in host organisms, as well as survival in the external milieu. Bacterial adaptation is accomplished through the coordinated activation of many different sensory receptors, signal processing proteins, and an array of molecular ma-chinery designed to execute the appropriate reactions. Key control points for many of these behavioral responses are signal processing pathways based on an archetypal two-component paradigm. The primary sensing component of such a system is an autophosphorylating protein kinase, while thesecond component—the response regulator—becomesactivated after receiving the phosphoryl group from the first.“Two-component” systems have been identified in as many as 20 distinct bacterial signal transductionpathways, ranging over30 prokaryotic genera. Operations of the individual systems vary widely according to their specific tasks, but for response regulation, it is likely that they allutilize the same activation mechanism of Mg2+-dependent protein phosphorylation. The molecular logic behind preservation of a common signaling mechanism in so many different pathways may lie in the ability to modulate crosstalk, thereby achieving a complex, concerted measure of response.Although response regulators exhibit great diversity in their domain organization and full-length primary sequences, they all share similarity in their regulatorydomain. One member of this superfamily is CheY, the single domain regulator of the bacterial chemotaxis system. CheY is the only response regulator for which a detailed three-dimensional structure is known. In thisreport, the CheY molecule is presented as the structural model for the regulatory domains of all bacterial two-component systems. A multiple alignment of 79 regu-latory domain sequences is analyzed. The correlation of the