Functional homology of chemotactic methylesterases from Bacillus subtilis and Escherichia coli.
AUTOR(ES)
Nettleton, D O
RESUMO
The methylesterase enzyme from Bacillus subtilis was compared with that from Escherichia coli. Both enzymes were able to demethylate methyl-accepting chemotaxis proteins (MCPs) from the other organism and were similarly affected by variations in glycerol, magnesium ion, or pH. When attractants were added to a mixture of B. subtilis MCPs and E. coli methylesterase, the rate of demethylation was enhanced. Conversely, when attractants were added to a mixture of E. coli MCPs and B. subtilis methylesterase, the rate of demethylation was diminished. These effects are what would be expected if, in these in vitro systems, the MCPs determined the rate of demethylation. These data suggest that, although the enzymes are from evolutionarily divergent organisms and are different in size, they have considerable functional homology.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=209563Documentos Relacionados
- Functional expression of two Bacillus subtilis chromosomal genes in Escherichia coli.
- Characterization of the proton/glutamate symport protein of Bacillus subtilis and its functional expression in Escherichia coli.
- Purification and characterization of the Bacillus subtilis levanase produced in Escherichia coli.
- Expression of the Bacillus subtilis glutamine synthetase gene in Escherichia coli.
- Isolation of a developmental gene of Bacillus subtilis and its expression in Escherichia coli.