title: Chemotactic methyltransferase promotes adaptation to repellents in Bacillus subtilis.
abstract: Bacillus subtilis cheRB, which encodes the chemotactic methyltransferase, has been cloned and sequenced. CheRB is a polypeptide of 256 amino acids, with a predicted molecular mass of 28 kDa. A comparison of the predicted amino acid sequence of B. subtilis CheRB with that of Escherichia coli CheRE demonstrates that the two enzymes share 31% amino acid identity. The homology was functional in that the expression of cheBB in an E. coli cheRE null mutant made the bacteria Che+. In contrast to cheRE null mutants which show a strong smooth swimming bias, cheRB null mutants were predominantly tumbly. They respond to the addition and subsequent removal of attractant. They also respond to the addition of repellent but do not adapt; they resume prestimulus bias on removal of repellent. Tethering analysis of a culture of a cheRB null mutant revealed two distinct subpopulations, each demonstrating unique behaviors. One showed a strong clockwise flagellar rotation bias, whereas the other was more random. The latter phenotype may be due to a deficiency of CheB and may reflect an interaction of CheB and CheR. Measurements of CheB activity in the cheR null mutant showed them to be only 20% of wild type levels. We conclude from this work that CheRB functions to promote adaptation to repellent stimuli in B. subtilis, whereas CheRE functions to promote adaptation to attractant stimuli in E. coli.
authors.affiliation: Department of Biochemistry, College of Medicine, University of Illinois, Urbana 61801.
authors.forename: M L
authors.initials: ML
authors.lastname: Kirsch
authors.forename: A R
authors.initials: AR
authors.lastname: Zuberi
authors.forename: D
authors.initials: D
authors.lastname: Henner
authors.forename: P D
authors.initials: PD
authors.lastname: Peters
authors.forename: M A
authors.initials: MA
authors.lastname: Yazdi
authors.forename: G W
authors.initials: GW
authors.lastname: Ordal
mesh_terms: D000064:Acclimatization; D000595:Amino Acid Sequence; D001383:Azetidinecarboxylic Acid / Q000494:pharmacology; D001412:Bacillus subtilis / Q000187:drug effects / Q000201:enzymology* / Q000502:physiology*; D001483:Base Sequence; D003001:Cloning, Molecular; D004926:Escherichia coli / Q000235:genetics; D015870:Gene Expression; D005798:Genes, Bacterial; D005816:Genetic Complementation Test; D005838:Genotype; D008715:Methionine / Q000378:metabolism; D008780:Methyltransferases / Q000235:genetics* / Q000378:metabolism*; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D010957:Plasmids; D015183:Restriction Mapping; D017386:Sequence Homology, Amino Acid
chemical_list: D001383:Azetidinecarboxylic Acid; D008715:Methionine; D008780:Methyltransferases; C038706:chemotaxis methyltransferase