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|Title:||Genetic, biochemical and behavioral studies of the chemotactic response in Bacillus subtilis|
|Author(s):||Kirsch, Michael Lee|
|Doctoral Committee Chair(s):||Ordal, George W.|
|Department / Program:||Biochemistry|
|Degree Granting Institution:||University of Illinois at Urbana-Champaign|
|Abstract:||The two enzymes involved in the major adaptation pathway of Bacillus subtilis chemotaxis were cloned and sequenced. They were found to be homologous to the corresponding enzymes of the Escherichia coli system. While the B. subtilis proteins could substitute for the E. coli proteins, they play opposite roles in the two organisms. CheB, the methylesterase, functions to promote adaptation to attractant stimuli in B. subtilis whereas it serves to promote adaptation to repellent stimuli in E. coli. CheR, the methyltransferase, functions to promote adaptation to repellent stimuli in B. subtilis whereas it serves to promote adaptation to attractant stimuli in E. coli. There exists another mechanism in B. subtilis which promotes adaptation to attractant stimuli but is independent of the methylation system. A methylation-independent adaptation system has been described for the E. coli system but it plays a much less significant role in that organism.
A cheR null mutant gives rise to two distinct subpopulations of cells which have different chemotactic phenotypes. A single bacterium always develops into the two different subpopulations. The behavior of one of the subpopulations is very similar to that of the double cheB/cheR mutant. Furthermore CheB activity is diminished when CheR is missing, as in the cheR mutant, or when there is an excess of CheR, as in the wild-type strain which overexpresses cheR.
|Rights Information:||Copyright 1994 Kirsch, Michael Lee|
|Date Available in IDEALS:||2011-05-07|
|Identifier in Online Catalog:||AAI9503239|
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