Research Topics
| H R KabackSummaryAffiliation: University of California Country: USA Publications
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Publications
The kamikaze approach to membrane transportH R Kaback
Howard Hughes Medical Institute, Department of Physiology, University of California, Los Angeles, California 90095 1662, USA
Nat Rev Mol Cell Biol 2:610-20. 2001..Novel approaches that have been developed and applied to one membrane transport protein, the lactose permease from Escherichia coli, are now being used to study various other membrane proteins...- Helix packing in polytopic membrane proteins: the lactose permease of Escherichia coliH R Kaback
Howard Hughes Medical Institute, Department of Physiology, University of California, Los Angeles 90024 1662, USA
Curr Opin Struct Biol 7:537-42. 1997..Using the lac permease as a paradigm, several site-directed biophysical and biochemical techniques are described which should be generally applicable... 
Ligand-induced conformational changes in the lactose permease of Escherichia coli: evidence for two binding sitesJ Wu
Department of Physiology, Howard Hughes Medical Institute, University of California at Los Angeles 90024 1662, USA
Protein Sci 3:2294-301. 1994..2 mM) does not alter quenching by either compound, whereas a higher concentration of ligand (10 mM) decreases the quenching constant for iodide by about 50% and for acrylamide by about 20%.(ABSTRACT TRUNCATED AT 250 WORDS)..- Cys-scanning mutagenesis: a novel approach to structure function relationships in polytopic membrane proteinsS Frillingos
Howard Hughes Medical Institute, Departments of Physiology and Microbiology and Molecular Genetics, Molecular Biology Institute, University of California Los Angeles, Los Angeles, California 90024
FASEB J 12:1281-99. 1998..structure-function relationships in polytopic membrane proteins... - The role of transmembrane domain III in the lactose permease of Escherichia coliM Sahin-Toth
Howard Hughes Medical Institute, Department of Physiology, University of California, Los Angeles 90024 1662, USA
Protein Sci 3:2302-10. 1994..The observations demonstrate that although no residue per se appears to be essential, structural properties of helix III are important for active lactose transport... - Characterization of Glu126 and Arg144, two residues that are indispensable for substrate binding in the lactose permease of Escherichia coliM Sahin-Toth
Howard Hughes Medical Institute, Department of Physiology, Molecular Biology Institute, University of California, Los Angeles 90095 1662, USA
Biochemistry 38:813-9. 1999..The results extend the conclusion that a carboxylate at position 126 and a guanidinium group at position 144 are irreplaceable for substrate binding and support the idea that Arg144 plays a major role in substrate specificity... - Dynamics of lactose permease of Escherichia coli determined by site-directed chemical labeling and fluorescence spectroscopyJ Wu
Howard Hughes Medical Institute, Department of Physiology and Microbiology, University of California, Los Angeles 90095 1662, USA
Biochemistry 34:8257-63. 1995..In striking contrast, mutants Pro28-->Cys and Pro31-->Cys react extremely slowly with MIANS in the absent of ligand, and TDG dramatically enhances reactivity.(ABSTRACT TRUNCATED AT 250 WORDS).. - Thiol cross-linking of transmembrane domains IV and V in the lactose permease of Escherichia coliC D Wolin
Howard Hughes Medical Institute, Departments of Physiology and of Microbiology and Molecular Genetics, Molecular Biology Institute, University of California, Los Angeles, Los Angeles, California 90025 1662, USA
Biochemistry 39:6130-5. 2000..The data provide strong support for the argument that Glu126 and Arg144 are within close proximity and suggest that an unpaired carboxylate at position 126 causes a structural change at the interface between helices IV and V... - Probing the conformation of the lactose permease of Escherichia coli by in situ site-directed sulfhydryl modificationS Frillingos
Howard Hughes Medical Institute, University of California, Los Angeles, 90024 1570, USA
Biochemistry 35:3950-6. 1996..In addition, the results are consistent with the idea that lactose permease has two binding sites: one with higher affinity on the periplasmic surface of the membrane and another with lower affinity on the cytoplasmic surface... - Ligand-induced changes in periplasmic loops in the lactose permease of Escherichia coliJ Sun
Howard Hughes Medical Institute, Department of Physiology, University of California, Los Angeles 90095 1662, USA
Biochemistry 37:8020-6. 1998.... - Proteomics on full-length membrane proteins using mass spectrometryJ le Coutre
Howard Hughes Medical Institute, Departments of Physiology and of Microbiology and Molecular Genetics, Molecular Biology Institute, University of California, Los Angeles 90095, USA
Biochemistry 39:4237-42. 2000..Finally, using in-line LC-MS, unknown proteins can be identified from solubilized Escherichia coli membranes without prior purification... - Properties of permease dimer, a fusion protein containing two lactose permease molecules from Escherichia coliM Sahin-Toth
Howard Hughes Medical Institute, Department of Physiology, University of California, Los Angeles 90024 1662
Proc Natl Acad Sci U S A 91:5421-5. 1994..The approach is consistent with the contention that the functional unit of lactose permease is a monomer... - In vitro folding of a membrane protein: effect of denaturation and renaturation on substrate binding by the lactose permease of Escherichia coliM M He
Howard Hughes Medical Institute, Department of Microbiology, University of California, Los Angeles 90095 1662, USA
Mol Membr Biol 15:15-20. 1998..The results demonstrate that both low- and high-affinity binding, as well as ligand-induced conformational changes in the permease, can be denatured reversibly in vitro... - Ligand-induced movement of helix X in the lactose permease from Escherichia coli: a fluorescence quenching studyQ Wang
Howard Hughes Medical Institute, Department of Physiology, Molecular Biology Institute, University of California, Los Angeles, Los Angeles, California 90024 1570, USA
Biochemistry 36:14120-7. 1997..R. (1997) Proc. Natl. Acad. Sci. U.S.A. 94, 5539-5543] in which substrate binding causes a conformational change resulting in movement of Glu325 to a nonpolar environment with a dramatic increase in pKa... - Helix packing in the lactose permease of Escherichia coli: distances between site-directed nitroxides and a lanthanideJ Voss
Chemistry Department, University of California, Davis, California 95616 0935, USA
Biochemistry 40:3184-8. 2001.... - A molecular mechanism for energy coupling in a membrane transport protein, the lactose permease of Escherichia coliH R Kaback
Howard Hughes Medical Institute, Department of Physiology, Molecular Biology Institute, University of California, Los Angeles, CA 90095 1662, USA
Proc Natl Acad Sci U S A 94:5539-43. 1997.... - The last two cytoplasmic loops in the lactose permease of Escherichia coli comprise a discontinuous epitope for a monoclonal antibodyJ Sun
Howard Hughes Medical Institute, Department of Physiology, University of California, Los Angeles 90095 1662, USA
Biochemistry 36:274-80. 1997.... - Interaction between residues Glu269 (helix VIII) and His322 (helix X) of the lactose permease of Escherichia coli is essential for substrate bindingM M He
Howard Hughes Medical Institute, Department of Physiology, University of California, Los Angeles 90095, USA
Biochemistry 36:13688-92. 1997..The observations are consistent with the notion that the interaction between Glu269 and His322 stabilizes the interface between helices V and VIII and thereby leads to binding of substrate... - Cysteine-scanning mutagenesis of transmembrane domain XII and the flanking periplasmic loop in the lactose permease of EScherichia coliM M He
Howard Hughes Medical Institute, Department of Physiology, University of California, Los Angeles 90095 1662, USA
Biochemistry 35:12909-14. 1996..Hubbell, W. L., & Kaback, H. R. (1996) Biochemistry 35, 12915-12918], site-directed spin labeling of single-Cys mutants at positions 387-402 is used to demonstrate that transmembrane domain XII is in an alpha-helical conformation... - Cysteine-scanning mutagenesis of helix II and flanking hydrophilic domains in the lactose permease of Escherichia coliS Frillingos
Howard Hughes Medical Institute, Department of Physiology, University of California, Los Angeles 90024 1570, USA
Biochemistry 36:269-73. 1997..The results demonstrate that although no residue per se in this region of the permease is irreplaceable, the surface of one face of helix II is important for active lactose transport... - Thiol cross-linking of cytoplasmic loops in the lactose permease of Escherichia coliI Kwaw
Howard Hughes Medical Institute, Departments of Physiology and of Microbiology and Molecular Genetics, Molecular Biology Institute, University of California, Los Angeles, California 90095 1662, USA
Biochemistry 39:3134-40. 2000..In addition, evidence is presented suggesting that ligand binding induces conformational alterations between loop IV/V and loop VIII/IX or X/XI... - Arg-302 facilitates deprotonation of Glu-325 in the transport mechanism of the lactose permease from EscherichiacoliM Sahin-Toth
Howard Hughes Medical Institute, Department of Physiology, Molecular Biology Institute, University of California, Los Angeles, CA 90095-1662, USA
Proc Natl Acad Sci U S A 98:6068-73. 2001..These observations lend strong support for the argument that Arg-302 interacts with Glu-325 to facilitate deprotonation of the carboxylic acid during turnover... - Effect of the lipid phase transition on the lactose permease from Escherichia coliW Zhang
Howard Hughes Medical Institute, Departments of Physiology and Microbiology and Molecular Genetics, Molecular Biology Institute, University of California Los Angeles, Los Angeles, California 90095 1662, USA
Biochemistry 39:14538-42. 2000.... - Tilting of helix I and ligand-induced changes in the lactose permease determined by site-directed chemical cross-linking in situJ Wu
Howard Hughes Medical Institute, Molecular Biology Institute, University of California, Los Angeles 90095 1662, USA
Biochemistry 37:15785-90. 1998..Taken together, the results indicate that ligand binding induces a translational or scissors-like rigid body movement of helix I and/or VII at the periplasmic interface between the helices... - Helix packing of lactose permease in Escherichia coli studied by site-directed chemical cleavageJ Wu
Howard Hughes Medical Institute, Department of Physiology, University of California, Los Angeles 90095 1662, USA
Proc Natl Acad Sci U S A 92:9186-90. 1995..The results suggest that helix V is in close proximity to helices VII and VIII with position 148 in the interface between the helices, position 149 facing helix VII, and position 147 facing the lipid bilayer... - Site-directed sulfhydryl labeling of the lactose permease of Escherichia coli: helices IV and V that contain the major determinants for substrate bindingI Kwaw
Howard Hughes Medical Institute, Department of Physiology and Microbiology, Molecular Biology Institute, University of California Los Angeles, Los Angeles, California 90095-1662, USA
Biochemistry 40:10491-9. 2001..Furthermore, positions that exhibit ligand-induced changes are located for the most part in the vicinity of the residues directly involved in substrate binding, as well as the cytoplasmic loop between helices IV and V... - Estimating loop-helix interfaces in a polytopic membrane protein by deletion analysisC D Wolin
Howard Hughes Medical Institute, Department of Physiology, Los Angeles, California 90025 1662, USA
Biochemistry 38:8590-7. 1999..More specifically, evidence is presented supporting the contention that Glu126 and Arg144 which are charge paired and critical for substrate binding are within helices IV and V, respectively... - Membrane topology of helices VII and XI in the lactose permease of Escherichia coli studied by lacY-phoA fusion analysis and site-directed spectroscopyM L Ujwal
Howard Hughes Medical Institute, Department of Physiology, Los Angeles, California, USA
Biochemistry 34:14909-17. 1995.... - Chemical rescue of Asp237-->Ala and Lys358-->Ala mutants in the lactose permease of Escherichia coliS Frillingos
Howard Hughes Medical Institute, Department of Physiology, University of California, Los Angeles 90024 1570, USA
Biochemistry 35:13363-7. 1996.... - Proximity of periplasmic loops in the lactose permease of Escherichia coli determined by site-directed cross-linkingJ Sun
Howard Hughes Medical Institute, Department of Physiology, Molecular Biology Institute, University of California at Los Angeles, Los Angeles, California 90095 1662, USA
Biochemistry 36:11959-65. 1997..U.S.A. 93, 14498-502] demonstrating that helices I and II are close to helices VII and XI. Finally, evidence is presented indicating that conformational flexibility between loops I/II and XI/XII may be important for permease turnover... - Functional estimation of loop-helix boundaries in the lactose permease of Escherichia coli by single amino acid deletion analysisC D Wolin
Howard Hughes Medical Institute, Department of Physiology, Molecular Biology Institute, University of California, Los Angeles, Los Angeles, California 90025-1662, USA
Biochemistry 40:1996-2003. 2001..Thus, transmembrane domain VI which is probably on the periphery of the 12-helix bundle may make few functionally important contacts... - Helix packing in the lactose permease of Escherichia coli: localization of helix VIL Guan
Howard Hughes Medical Institute, University of California Los Angeles, Los Angeles, CA 90095 1662, USA
J Mol Biol 312:69-77. 2001.... - The C-4 hydroxyl group of galactopyranosides is the major determinant for ligand recognition by the lactose permease of Escherichia coliM Sahin-Toth
Howard Hughes Medical Institute, University of California Los Angeles, Los Angeles, California 90095 1662, USA
Biochemistry 40:13015-9. 2001..Moreover, the C-4 hydroxyl is identified as the major determinant of ligand binding, suggesting that sugar recognition in lactose permease may have evolved to discriminate primarily between gluco- and galactopyranosides... - Functional complementation of internal deletion mutants in the lactose permease of Escherichia coliE Bibi
Howard Hughes Medical Institute, Department of Physiology, University of California, Los Angeles 90024 1574
Proc Natl Acad Sci U S A 89:1524-8. 1992.... - Functional interactions between putative intramembrane charged residues in the lactose permease of Escherichia coliM Sahin-Toth
Howard Hughes Medical Institute, Department of Physiology, University of California, Los Angeles 90024 1574
Proc Natl Acad Sci U S A 89:10547-51. 1992..In any event, the findings suggest that putative transmembrane helix VII lies next to helices X and XI in the tertiary structure of lactose permease... - Toward the bilayer proteome, electrospray ionization-mass spectrometry of large, intact transmembrane proteinsJ P Whitelegge
Department of Chemistry and Biochemistry, University of California, Los Angeles, CA 90095, USA
Proc Natl Acad Sci U S A 96:10695-8. 1999..Furthermore, ESI-MS is used to titrate reactive thiols with N-ethylmaleimide. Treatment of the native protein solubilized in detergent micelles reveals only two reactive thiols, and both are protected by a substrate analog... - The lac permease of Escherichia coli: a prototypic energy-transducing membrane proteinH R Kaback
Howard Hughes Medical Institute, University of California, Los Angeles 90024-1570
Biochim Biophys Acta 1018:160-2. 1990 - Isolation and functional reconstitution of soluble melibiose permease from Escherichia coliP D Roepe
Howard Hughes Medical Institute, University of California, Los Angeles 90024 1574
Biochemistry 29:2572-7. 1990.... - Fourier transform infrared spectroscopy reveals a rigid alpha-helical assembly for the tetrameric Streptomyces lividans K+ channelJ le Coutre
Howard Hughes Medical Institute, Departments of Physiology and Microbiology and Molecular Genetics, Molecular Biology Institute, University of California, Los Angeles, CA 90095 1662, USA
Proc Natl Acad Sci U S A 95:6114-7. 1998..On average, the alpha-helices are tilted 33 degrees normal to the membrane surface. The results are discussed in relationship to the lactose permease of Escherichia coli, a membrane transport protein... - Membrane topology of the melibiose permease of Escherichia coli studied by melB-phoA fusion analysisT Pourcher
Laboratoire J Maetz, Département de Biologie Cellulaire et Moléculaire CEA, France
Biochemistry 35:4161-8. 1996.... - Engineering the lac permease for purification and crystallizationG G Prive
Ontario Cancer Institute, University of Toronto, Canada
J Bioenerg Biomembr 28:29-34. 1996..The "red permease" is very easy to monitor through the steps of expression, purification, concentration, and crystallization... - Deduction of consensus binding sequences on proteins that bind IIAGlc of the phosphoenolpyruvate:sugar phosphotransferase system by cysteine scanning mutagenesis of Escherichia coli lactose permeaseM Sondej
Laboratory of Biochemical Genetics, National Heart, Lung and Blood Institute, National Institutes of Health, Bethesda, MD 20892, USA
Proc Natl Acad Sci U S A 96:3525-30. 1999..The requirement for two interaction regions is interpreted in the regulatory framework of a substrate-dependent conformational change that brings those two regions into an orientation optimal for binding IIAGlc... - Topology of allosteric regulation of lactose permeaseY J Seok
Laboratory of Biochemical Genetics, National Heart, Lung and Blood Institute, Bethesda, MD 20892 4036, USA
Proc Natl Acad Sci U S A 94:13515-9. 1997..A topological map of the proposed interaction is presented... - Cloning and functional expression in bacteria of a novel glucose transporter present in liver, intestine, kidney, and beta-pancreatic islet cellsB Thorens
Whitehead Institute for Biomedical Research, Cambridge, Massachusetts 02142
Cell 55:281-90. 1988..Insulinoma cells express, inappropriately, the erythrocyte glucose transporter, and we suggest that this may be related to their inability to secrete insulin in response to elevations in glucose... - Vinylglycolate resistance in Escherichia coliL Shaw
J Bacteriol 121:1047-55. 1975..This indicates that vinylglycolate is oxidized to 2-keto-3-butenoate before inactivating the phosphoenolpyruvate-dependent phosphotransferase system. These results were found in whole cells and confirmed in isolated membrane vesicles...