Biomaterial Database

Cloning and characterization of genes encoding methyl-accepting chemotaxis proteins in Bacillus subtilis. 1994

D W Hanlon, and G W Ordal

Department of Biochemistry, Colleges of Medicine and Liberal Arts and Sciences, University of Illinois, Urbana 61801.

Several genes homologous to the methyl-accepting chemotaxis proteins (MCPs) of Escherichia coli have been cloned and characterized from the Gram-positive bacterium, Bacillus subtilis. Sequence analysis reveals four large open reading frames, designated mcpA, mcpB, tlpA, and tlpB, each encoding a predicted 72-kDa protein. These proteins exhibit strong homology to chemoreceptors from several organisms, although similarity is limited to the C-terminal domain. These transducer genes were mapped to a chromosomal position of 279 degrees, which is distant from previously identified fla, mot, or che loci. Each gene was inactivated by insertion of a nonpolar chloramphenicol acetyltransferase cassette in the N-terminal region. In vivo methylation of the bacterial strain deficient in mcpA revealed the loss of several methylated bands in the range of the MCP previously designated as H1, and greatly reduced methylation of the MCP designated as H2. Furthermore, this bacterial strain exhibited a chemotaxis deficiency toward glucose and alpha-methyl-glucoside. Inactivation of mcpB caused a reduction in methylation of the MCP designated as H3, while chemotaxis toward asparagine, aspartate, glutamine, and histidine was significantly impaired in this strain. Despite strong homology, inactivation of tlpA and tlpB did not result in an observed deficiency in chemotaxis. Most unusually, these mutant strains exhibited a striking tendency to adhere together and resisted disaggregation.

UI	MeSH Term	Description	Entries
D008565	Membrane Proteins	Proteins which are found in membranes including cellular and intracellular membranes. They consist of two types, peripheral and integral proteins. They include most membrane-associated enzymes, antigenic proteins, transport proteins, and drug, hormone, and lectin receptors.	Cell Membrane Protein,Cell Membrane Proteins,Cell Surface Protein,Cell Surface Proteins,Integral Membrane Proteins,Membrane-Associated Protein,Surface Protein,Surface Proteins,Integral Membrane Protein,Membrane Protein,Membrane-Associated Proteins,Membrane Associated Protein,Membrane Associated Proteins,Membrane Protein, Cell,Membrane Protein, Integral,Membrane Proteins, Integral,Protein, Cell Membrane,Protein, Cell Surface,Protein, Integral Membrane,Protein, Membrane,Protein, Membrane-Associated,Protein, Surface,Proteins, Cell Membrane,Proteins, Cell Surface,Proteins, Integral Membrane,Proteins, Membrane,Proteins, Membrane-Associated,Proteins, Surface,Surface Protein, Cell
D008745	Methylation	Addition of methyl groups. In histo-chemistry methylation is used to esterify carboxyl groups and remove sulfate groups by treating tissue sections with hot methanol in the presence of hydrochloric acid. (From Stedman, 25th ed)	Methylations
D008969	Molecular Sequence Data	Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.	Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D009154	Mutation	Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.	Mutations
D009838	Oligodeoxyribonucleotides	A group of deoxyribonucleotides (up to 12) in which the phosphate residues of each deoxyribonucleotide act as bridges in forming diester linkages between the deoxyribose moieties.	Oligodeoxynucleotide,Oligodeoxyribonucleotide,Oligodeoxynucleotides
D002633	Chemotaxis	The movement of cells or organisms toward or away from a substance in response to its concentration gradient.	Haptotaxis
D003001	Cloning, Molecular	The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.	Molecular Cloning
D004269	DNA, Bacterial	Deoxyribonucleic acid that makes up the genetic material of bacteria.	Bacterial DNA
D005798	Genes, Bacterial	The functional hereditary units of BACTERIA.	Bacterial Gene,Bacterial Genes,Gene, Bacterial
D000072236	Methyl-Accepting Chemotaxis Proteins	Transmembrane sensor receptor proteins that are central components of the chemotactic systems of a number of motile bacterial species which include ESCHERICHIA COLI and SALMONELLA TYPHIMURIUM. Methyl-accepting chemotaxis proteins derive their name from a sensory adaptation process which involves methylation at several glutamyl residues in their cytoplasmic domain. Methyl-accepting chemotaxis proteins trigger chemotactic responses across spatial chemical gradients, causing organisms to move either toward favorable stimuli or away from toxic ones.	Methyl-Accepting Chemotaxis Protein,MACP-I,MACP-II,Methyl Accepting Chemotaxis Protein 1,Methyl Accepting Chemotaxis Protein 2,Methyl Accepting Chemotaxis Protein 3,Methyl-Accepting Chemotaxis Protein I,Methyl-Accepting Chemotaxis Protein II,Methyl-Accepting Chemotaxis Protein III,Chemotaxis Protein, Methyl-Accepting,Chemotaxis Proteins, Methyl-Accepting,Methyl Accepting Chemotaxis Protein,Methyl Accepting Chemotaxis Protein I,Methyl Accepting Chemotaxis Protein II,Methyl Accepting Chemotaxis Protein III,Methyl Accepting Chemotaxis Proteins,Protein, Methyl-Accepting Chemotaxis,Proteins, Methyl-Accepting Chemotaxis