JBC INTERFERin siRNA transfection reagent

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Botfield, M. C.
Right arrow Articles by Wilson, T. H.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Botfield, M. C.
Right arrow Articles by Wilson, T. H.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

J. Biol. Chem., Vol. 263, Issue 26, 12909-12915, Sep, 1988

Mutations that simultaneously alter both sugar and cation specificity in the melibiose carrier of Escherichia coli

MC Botfield and TH Wilson
Department of Cellular and Molecular Physiology, Harvard Medical School, Boston, Massachusetts 02115.

The isolation and deduced amino acid sequence of 70 melibiose carrier mutants with impaired methyl-beta-D-galactopyranoside (TMG) and cation recognition properties is described. The Km for TMG transport ranged from 1 to greater than 100 mM. Amino acid substitutions occurred at 23 unique sites within the protein. These sites were clustered into four distinct regions: Asp-15 through Ile-18 (cluster I), Tyr-116 through Pro-122 (cluster II), Val-342 through Ile-348 (cluster III), and Ala- 364 through Gly-374. Only two sites fell outside of these clusters: Ile- 61 and Ala-236. In the native conformation, some or all of these clusters may interact to form the substrate recognition site. Impairment of TMG recognition was accompanied by decreased Li+ inhibition of melibiose transport in all but one mutant. That changes in sugar recognition properties should so frequently accompany changes in cation recognition properties suggests an interaction between the two substrates. A model for such interaction is proposed.
Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
 Biophys. JHome page
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]

Home page
 J. Biol. Chem.Home page
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]

Home page
 J. Biol. Chem.Home page
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]

Home page
 J. Biol. Chem.Home page
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]

Home page
 J. Bacteriol.Home page
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]

Home page
 J. Biol. Chem.Home page
J. A. Hall, M.-C. Fann, and P. C. Maloney
Altered Substrate Selectivity in a Mutant of an Intrahelical Salt Bridge in UhpT, the Sugar Phosphate Carrier of Escherichia coli
J. Biol. Chem., March 5, 1999; 274(10): 6148 - 6153.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
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]

Home page
 J. Biol. Chem.Home page
E. Cordat, I. Mus-Veteau, and G. Leblanc
Structural Studies of the Melibiose Permease of Escherichia coli by Fluorescence Resonance Energy Transfer. II. IDENTIFICATION OF THE TRYPTOPHAN RESIDUES ACTING AS ENERGY DONORS
J. Biol. Chem., December 11, 1998; 273(50): 33198 - 33202.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
L. M. Veenhoff, E. R. Geertsma, J. Knol, and B. Poolman
Close Approximation of Putative alpha -Helices II, IV, VII, X, and XI in the Translocation Pathway of the Lactose Transport Protein of Streptococcus thermophilus
J. Biol. Chem., July 28, 2000; 275(31): 23834 - 23840.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 1988 by the American Society for Biochemistry and Molecular Biology.