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3. Probing the binding domain of the saccharomyces cerevisiae alpha-mating factor receptor with fluorescent ligands

Author

Ding, Fa-Xiang, Lee, B.K., Hauser, M., Davenport, Lesley, Becker, J.M., and Naider, F.

Subjects
Saccharomyces -- Research, Pheromones -- Physiological aspects, Binding sites (Biochemistry) -- Analysis, Protein binding -- Physiological aspects, Biological sciences, Chemistry
Abstract

Results show that the 7-nitrobenz-2-oxa-1,3-diazol-4-yl group is the binding domain of alpha-mating pheromone factor of Saccharomyces cerevisiae as revealed by the changes in the fluorescence emission spectrum upon its binding to the receptor.

Published
2001

13. Expression and biophysical analysis of a triple-transmembrane domain-containing fragment from a yeast G protein-coupled receptor

Author

Caroccia, K E, Estephan, R, Cohen, L S, Arshava, B, Hauser, M, Zerbe, O, Becker, J M, Naider, F, University of Zurich, and Naider, F

Subjects
10120 Department of Chemistry, 1303 Biochemistry, Molecular Sequence Data, Biophysics, Saccharomyces cerevisiae, Biochemistry, Mass Spectrometry, Protein Structure, Secondary, Receptors, G-Protein-Coupled, Biomaterials, 03 medical and health sciences, GPCR, 540 Chemistry, Amino Acid Sequence, Nuclear Magnetic Resonance, Biomolecular, Chromatography, High Pressure Liquid, 030304 developmental biology, 0303 health sciences, Circular Dichroism, 2502 Biomaterials, 030302 biochemistry & molecular biology, Organic Chemistry, General Medicine, NMR, Peptide Fragments, Electrophoresis, Polyacrylamide Gel, 1304 Biophysics, 1605 Organic Chemistry
Abstract

Structural characterization of G protein-coupled receptors (GPCRs) is hindered by the inherent hydrophobicity, flexibility, and large size of these signaling proteins. Insights into conformational preferences and the three-dimensional (3D) structure of domains of these receptors can be obtained using polypeptide fragments of these proteins. Herein, we report the expression, purification, and biophysical characterization of a three-transmembrane domain-containing 131-residue fragment of the yeast α-factor receptor, Ste2p. Ste2p TM1–TM3 (G31–R161) was expressed as a TrpΔLE fusion protein in Escherichia coli. The expressed protein was subject to CNBr cleavage to remove the fusion tag and TM1–TM3 was purified by reverse-phased HPLC. The cleavage product was isolated in yields of up to 20 mg per liter of culture in both unlabeled and uniformly [15N]-labeled and [15N, 13C, 2H]-labeled forms. The secondary structure of TM1–TM3 was determined to be helical in a number of membrane mimetic environments, including 2,2,2-trifluoroethanol (TFE):water and lysomyristoylphosphatidylglycerol (LMPG) detergent micelles by circular dichroism. Preliminary HSQC analysis in 50% TFE:water and LMPG micelles prepared in sodium phosphate and 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid (HEPES) buffers revealed that this fragment is suitable for structural analysis by nuclear magnetic resonance (NMR). Complete backbone assignments and a detailed localization of the secondary structural elements of TM1–TM3 in 50% TFE:water have been achieved.

Published
2011
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15. Expression and biophysical analysis of two double transmembrane domain-containing fragments from a yeast G protein-coupled receptor

Author

Cohen, L S, Arshava, B, Estephan, R, Englander, J, Kim, H, Hauser, M, Zerbe, O, Ceruso, M, Becker, J M, Naider, F, University of Zurich, and Naider, F

Subjects
10120 Department of Chemistry, 1303 Biochemistry, 540 Chemistry, 2502 Biomaterials, 1304 Biophysics, 1605 Organic Chemistry, membrane peptides • double transmembrane domains • GPCRs • expression of peptides • NMR in detergents
Published
2008

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