Interaction of the maltose-binding protein with membrane vesicles of Escherichia coli.
AUTOR(ES)
Richarme, G
RESUMO
The interaction of the radioactively labeled purified maltose-binding protein of Escherichia coli with membrane vesicles was studied. The maltose-binding protein bound specifically to the vesicles, in the presence of maltose, on few sites. Under conditions in which a potential was imposed across the membrane, the specific binding was (i) increased, (ii) dependent on maltose, and (iii) abolished in a mutant defective in the tar gene product, one of the methyl-accepting chemotaxis proteins. At least 1,300 binding sites were present in the membrane fraction of logarithmically growing cells.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=216556Documentos Relacionados
- Periplasmic maltose-binding protein confers specificity on the outer membrane maltose pore of Escherichia coli.
- Active transport of maltose in membrane vesicles obtained from Escherichia coli cells producing tethered maltose-binding protein.
- Electrochemical potential releases a membrane-bound secretion intermediate of maltose-binding protein in Escherichia coli.
- Maltose chemoreceptor of Escherichia coli: interaction of maltose-binding protein and the tar signal transducer.
- Mutations that improve export of maltose-binding protein in SecB- cells of Escherichia coli.