NDLI: Cooperative binding of lactose and the phosphorylated phosphocarrier protein HPr(Ser-P) to the lactose/H+ symport permease of Lactobacillus brevis.

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Cooperative binding of lactose and the phosphorylated phosphocarrier protein HPr(Ser-P) to the lactose/H+ symport permease of Lactobacillus brevis.

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Cooperative binding of lactose and the phosphorylated phosphocarrier protein HPr(Ser-P) to the lactose/H+ symport permease of Lactobacillus brevis.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Saier, M. H. Ye, J. J.
Description	Author Affiliation: Ye JJ ( Department of Biology, University of California at San Diego, La Jolla 92093-0116.);
Abstract	Lactobacillus brevis accumulates lactose and nonmetabolizable lactose analogues via sugar/H+ symport, but addition of glucose to the extracellular medium results in rapid efflux of the free sugar from the cells due to the uncoupling of sugar transport from proton transport. By using vesicles of L. brevis cells, we recently showed that these regulatory/effects could be attributed to the metabolite-activated ATP-dependent protein kinase-catalyzed phosphorylation of serine-46 in the phosphocarrier protein HPr [HPr(Ser-P)] of the phosphotransferase system and that a mutant form of HPr with the serine-46-->aspartate replacement ([S46D]HPr) is apparently locked in the seryl phosphorylated conformation. We here demonstrate that [S46D]HPr binds directly to inside-out membrane vesicles of L. brevis that contain the lactose permease. Sugar substrates of the permease markedly and specifically stimulate binding of [S46D]HPr to the membranes while certain transport inhibitors such as N-ethylmaleimide block binding. The pH dependency for binding follows that for transport. Wild-type HPr and the [S46A]HPr mutant protein did not appreciably compete with [S46D]HPr for binding to the permease. These results provide evidence for the direct interaction of HPr(Ser-P) with an allosteric site on the lactose/proton symporter of L. brevis for the purpose of regulating sugar accumulation in response to the metabolic needs of the cell.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	2
Volume Number	92
Language	English
Publisher	National Academy of Sciences
Publisher Date	1995-02-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Bacterial Proteins Carrier Proteins Metabolism Escherichia Coli Proteins Lactobacillus Lactose Monosaccharide Transport Proteins Phosphoenolpyruvate Sugar Phosphotransferase System Symporters Allosteric Regulation Binding, Competitive Biological Transport Drug Effects Ethylmaleimide Pharmacology Iodine Radioisotopes Isopropyl Thiogalactoside Isotope Labeling Enzymology Melibiose Membranes Phosphorylation Phosphoserine Protein Binding Thiogalactosides Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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