University of Illinois Urbana-Champaign

Chemotaxis Methyltransferase Ii From Bacillus Subtilis

Burgess-Cassler, Anthony

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Description

Title
Chemotaxis Methyltransferase Ii From Bacillus Subtilis
Author(s)
Burgess-Cassler, Anthony
Issue Date
1983
Department of Study
Biochemistry
Discipline
Biochemistry
Degree Granting Institution
University of Illinois at Urbana-Champaign
Degree Name
Ph.D.
Degree Level
Dissertation
Keyword(s)
Chemistry, Biochemistry
Abstract
  • Chemotaxis is the process by which motile cells sense and respond to their chemical environment. Following a period of time during which chemotactic bacteria respond to chemical stimulation, they revert to their pre-stimulus behavior, or adapt. Biochemically, adaptation is correlated with the methylation or demethylation of certain integral membrane proteins, the methyl-accepting chemotaxis proteins (MCPs). We have purified and characterized a chemotaxis methyltransferase (methyltransferase II) from Bacillus subtilis. By using a combination of DEAE Bio-Gel A chromatography, CM Bio-Gel A chromatography, ammonium sulfate fractionation, and S-adenosylhomocysteine affinity chromatography, a virtually homogeneous product was obtained.
  • The enzyme was shown to be a monomer with a native molecular weight of 30,000, a K(,m) for S-adenosylmethionine of 5 (mu)M, and a K(,i) for S-adenosylhomocysteine of 0.2 (mu)M. The MCP methylation reaction in vitro was activated by divalent cation and inhibited by NaCl or KCl. It had a pH optimum of 7 and a temperature optimum of 20-25(DEGREES)C. The linkage between the MCP and the transferred methyl group was preliminarily characterized as gammaglutamyl methyl ester.
  • Methyltransferase II appeared to have the ability to gain access to the intracellular space in permeabilization assays. It was also determined that a 68,000 molecular weight cytoplasmic protein (with two sub-units) could serve as a methyltransferase II substrate. The cytoplasmic protein was partially purified and characterized.
  • Finally, functional homology between Bacillus subtilis methyl-transferase II and Escherichia coli cheR protein was established.
Graduation Semester
1983
Type of Resource
text
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http://hdl.handle.net/2142/70516

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