Maltose chemoreceptor of Escherichia coli: interaction of maltose-binding protein and the tar signal transducer

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Maltose chemoreceptor of Escherichia coli.

Strains carrying mutations in the maltose system of Escherichia coli were assayed for maltose taxis, maltose uptake at 1 and 10 muM maltose, and maltose-binding activity released by osmotic shock. An earlier conclusion that the metabolism of maltose is not necessary for chemoreception is extended to include the functioning of maltodextrin phosphorylase, the product of malP, and the genetic cont...

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Interaction of the maltose-binding protein with membrane vesicles of Escherichia coli.

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...

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Unliganded maltose-binding protein triggers lactose transport in an Escherichia coli mutant with an alteration in the maltose transport system.

Escherichia coli accumulates malto-oligosaccharides by the maltose transport system, which is a member of the ATP-binding-cassette (ABC) superfamily of transport systems. The proteins of this system are LamB in the outer membrane, maltose-binding protein (MBP) in the periplasm, and the proteins of the inner membrane complex (MalFGK2), composed of one MalF, one MalG, and two MalK subunits. Subst...

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Direct utilization of maltose by Escherichia coli.

In the course of genetic studies, a mutant strain of Escherichia coli was developed which is characterized by rapid fermentation and oxidat,ion of maltose but not of glucose. Since this mutant offered an excellent opportunity to invest,igate the so called direct utilization of disaccharides (l), a study of the enzyme systems involved in maltose decomposition was undertaken. Experiments with dry...

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The remarkable solubility-enhancing power of Escherichia coli maltose-binding protein.

A common problem encountered during the production of recombinant proteins, particularly in bacteria, is their tendency to accumulate in an insoluble and inactive form (i.e., as inclusion bodies). Although sometimes it is possible to convert the aggregated material into native, biologically active protein, this is a time-consuming, costly, and uncertain undertaking. Consequently, a general mean...

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ژورنال

عنوان ژورنال: Journal of Bacteriology

سال: 1988

ISSN: 0021-9193,1098-5530

DOI: 10.1128/jb.170.10.4516-4521.1988