HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Damiano-Forano, E. Articles by Leblanc, G. Search for Related Content PubMed PubMed Citation Articles by Damiano-Forano, E. Articles by Leblanc, G. Social Bookmarking                      What's this?

J. Biol. Chem., Vol. 261, Issue 15, 6893-6899, May, 1986

Sugar binding properties of the melibiose permease in Escherichia coli membrane vesicles. Effects of Na+ and H+ concentrations

E Damiano-Forano, M Bassilana and G Leblanc

The substrate binding reaction of the melibiose carrier was analyzed by studying [3H]p-nitrophenyl-alpha-D-galactopyranoside (Np alpha Gal) binding to de-energized membrane vesicles from Escherichia coli RA11 as a function of H+ and Na+ (or Li+) concentrations. The data indicate first that Na+ (or Li+) activates Np alpha Gal binding at all pH values tested between 5.5 and 7.5 and second that H+ inhibits the Na+ (or Li+)- dependent activating effect on Np alpha Gal binding. Similar conclusions were drawn for melibiose and methyl-1-thio-beta-D- galactoside binding activities. Unexpectedly, Np alpha Gal, melibiose, and methyl-1-thio-beta-D-galactoside binding activities are insensitive to a variety of SH reagents which completely block transport activity. Quantitative analysis of the effects of H+ and Na+ ions on the parameters of Np alpha Gal binding show that 1) the maximal number of binding sites is constant irrespective of the concentration of Na+ or Li+ in the range of pH between 6 and 7.5 and 2) the apparent dissociation constant for Np alpha Gal binding varies with both Na+ and H+ according to a relation described by a linear combination of the concentration of H+ and the reciprocal of Na+ concentration. These results can be accounted for by a model which assumes sequential binding of the cation and substrate in this order and competition between Na+ and H+ for a common cationic binding site on the porter. Predictions of the proposed binding model for a carrier mechanism catalyzing sugar transport according to a Na+ symport mode or a H+ symport mode are discussed.
CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				N. Dave, V. A. Lorenz-Fonfria, G. Leblanc, and E. Padros FTIR Spectroscopy of Secondary-Structure Reorientation of Melibiose Permease Modulated by Substrate Binding Biophys. J., May 1, 2008; 94(9): 3659 - 3670. [Abstract] [Full Text] [PDF]

				X. Leon, R. Lemonnier, G. Leblanc, and E. Padros Changes in Secondary Structures and Acidic Side Chains of Melibiose Permease upon Cosubstrates Binding Biophys. J., December 15, 2006; 91(12): 4440 - 4449. [Abstract] [Full Text] [PDF]

				M. Quick, H. Yano, N. R. Goldberg, L. Duan, T. Beuming, L. Shi, H. Weinstein, and J. A. Javitch State-dependent Conformations of the Translocation Pathway in the Tyrosine Transporter Tyt1, a Novel Neurotransmitter:Sodium Symporter from Fusobacterium nucleatum J. Biol. Chem., September 8, 2006; 281(36): 26444 - 26454. [Abstract] [Full Text] [PDF]

				K. Meyer-Lipp, N. Sery, C. Ganea, C. Basquin, K. Fendler, and G. Leblanc The Inner Interhelix Loop 4-5 of the Melibiose Permease from Escherichia coli Takes Part in Conformational Changes after Sugar Binding J. Biol. Chem., September 8, 2006; 281(36): 25882 - 25892. [Abstract] [Full Text] [PDF]

				M. A. Dayem, C. Basquin, T. Pourcher, E. Cordat, and G. Leblanc Cytoplasmic Loop Connecting Helices IV and V of the Melibiose Permease from Escherichia coli Is Involved in the Process of Na+-coupled Sugar Translocation J. Biol. Chem., January 10, 2003; 278(3): 1518 - 1524. [Abstract] [Full Text] [PDF]

				N. Dave, V. A. Lorenz-Fonfria, J. Villaverde, R. Lemonnier, G. Leblanc, and E. Padros Study of Amide-proton Exchange of Escherichia coli Melibiose Permease by Attenuated Total Reflection-Fourier Transform Infrared Spectroscopy. EVIDENCE OF STRUCTURE MODULATION BY SUBSTRATE BINDING J. Biol. Chem., January 25, 2002; 277(5): 3380 - 3387. [Abstract] [Full Text] [PDF]

				P. J. Franco and T. H. Wilson Arg-52 in the Melibiose Carrier of Escherichia coli Is Important for Cation-Coupled Sugar Transport and Participates in an Intrahelical Salt Bridge J. Bacteriol., October 15, 1999; 181(20): 6377 - 6386. [Abstract] [Full Text]

				C. Maehrel, E. Cordat, I. Mus-Veteau, and G. Leblanc Structural Studies of the Melibiose Permease of Escherichia coli by Fluorescence Resonance Energy Transfer. I. EVIDENCE FOR ION-INDUCED CONFORMATIONAL CHANGE J. Biol. Chem., December 11, 1998; 273(50): 33192 - 33197. [Abstract] [Full Text] [PDF]