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The molecular analysis and characterization of chemotaxis genes in Bacillus subtilis

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Title: The molecular analysis and characterization of chemotaxis genes in Bacillus subtilis
Author(s): Bischoff, David Scott
Doctoral Committee Chair(s): Ordal, George W.
Department / Program: Biochemistry
Discipline: Biochemistry
Degree Granting Institution: University of Illinois at Urbana-Champaign
Degree: Ph.D.
Genre: Dissertation
Subject(s): Biology, Molecular Biology, Genetics Chemistry, Biochemistry
Abstract: Bacteria sense their environment and alter their behavior in order to migrate towards more favorable conditions. Some of the genes involved in this chemotactic process in Bacillus subtilis have been cloned, sequenced and inactivated in order to understand the mechanism controlling this behavior. All the genes that were inactivated are present in a single transcription unit in B. subtilis. Many of these genes encoded proteins that were homologous to Escherichia coli flagellar structural, biosynthetic, and chemotaxis proteins.One of the genes, cheY, is the B. subtilis homolog of the tumble regulator in E. coli that transmits the signal to the flagellar switch and causes the bacteria to tumble. Although these proteins are homologous, inactivation of B. subtilis cheY implies that they have different roles in the two organisms. B. subtilis CheY is required under certain circumstances for both smooth swimming and tumbling, rather than for just tumbling as in E. coli. B. subtilis CheY also has an effect on the methylation of the membrane bound methyl-accepting chemotaxis proteins, possibly due to interaction with an unidentified methylated regulator at the switch or as a feedback mechanism for adaptation to the chemotactic stimuli. Two other genes, fliM and fliY, encode proteins that are components of the switch complex in B. subtilis that controls the direction of rotation of the flagella. The other three genes encode proteins that are involved in synthesis of the flagella. FliP and FliQ are flagellar biosynthetic proteins. FliZ is thought to be a structural component that anchors the flagella to the membrane.
Issue Date: 1992
Type: Text
Language: English
URI: http://hdl.handle.net/2142/19658
Rights Information: Copyright 1992 Bischoff, David Scott
Date Available in IDEALS: 2011-05-07
Identifier in Online Catalog: AAI9236398
OCLC Identifier: (UMI)AAI9236398
 

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