Evidence for methyl group transfer between the methyl-accepting chemotaxis proteins in Bacillus subtilis.
AUTOR(ES)
Bedale, W A
RESUMO
We present evidence for methyl (as methyl or methoxy) transfer from the methyl-accepting chemotaxis proteins H1 and possibly H3 of Bacillus subtilis to the methyl-accepting chemotaxis protein H2. This methyl transfer, which has been observed in vitro (D. J. Goldman and G. W. Ordal, Biochemistry 23:2600-2606, 1984), was strongly stimulated by the chemoattractant aspartate and thus may play an important role in the sensory processing system of this organism. Although radiolabeling of H1 and H3 began at once after the addition of [3H]methionine, radiolabeling of H2 showed a lag. Furthermore, the addition of excess nonradioactive methionine caused immediate exponential delabeling of H1 and H3 while labeling of H2 continued to increase. Methylation of H2 required the chemotactic methyltransferase, probably to first methylate H1 and H3. Aspartate caused increased labeling of H2 and strongly decreased labeling of H1 and H3 after the addition of nonradioactive methionine. Without the addition of nonradioactive methionine, aspartate caused demethylation of H1 and to a lesser extent H3, with an approximately equal increase of methylation of H2.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=210630Documentos Relacionados
- Influence of attractants and repellents on methyl group turnover on methyl-accepting chemotaxis proteins of Bacillus subtilis and role of CheW.
- Posttranslational processing of methyl-accepting chemotaxis proteins in Escherichia coli
- Structural studies of methyl-accepting chemotaxis proteins of Escherichia coli: evidence for multiple methylation sites.
- Methyl-accepting taxis proteins in Halobacterium halobium.
- Genetics of methyl-accepting chemotaxis proteins in Escherichia coli: organization of the tar region.