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Volumn 76, Issue 2, 2004, Pages 119-128

Sexual Conjugation in Yeast: A Paradigm to Study G-Protein-Coupled Receptor Domain Structure

Author keywords

[No Author keywords available]

Indexed keywords

DIPLOID CELLS; HAPLOIDS;

EID: 1942435227     PISSN: 00063525     EISSN: None     Source Type: Journal    
DOI: 10.1002/bip.10567     Document Type: Conference Paper
Times cited : (16)

References (38)
  • 2
    • 0038024615 scopus 로고    scopus 로고
    • The G-protein-coupled receptors in the human genome form five main families. Phylogenetic analysis, paralogon groups, and fingerprints
    • Fredriksson, R.; Lagerstrom, M. C.; Lundin, L. G.; Schioth, H. B. The G-protein-coupled receptors in the human genome form five main families. Phylogenetic analysis, paralogon groups, and fingerprints. Mol Pharmacol 2003, 63, 1256-1272.
    • (2003) Mol Pharmacol , vol.63 , pp. 1256-1272
    • Fredriksson, R.1    Lagerstrom, M.C.2    Lundin, L.G.3    Schioth, H.B.4
  • 3
    • 0037189901 scopus 로고    scopus 로고
    • Four-dimensional NMR spectroscopy of a 723-residue protein Chemical shift assignments and secondary structure of malate synthase g
    • Tugarinov, V.; Muhandiram, R.; Ayed, A.; Kay, L. E. Four-dimensional NMR spectroscopy of a 723-residue protein: Chemical shift assignments and secondary structure of malate synthase g. J Am Chem Soc 2002, 124, 10025-10035.
    • (2002) J Am Chem Soc , vol.124 , pp. 10025-10035
    • Tugarinov, V.1    Muhandiram, R.2    Ayed, A.3    Kay, L.E.4
  • 6
    • 0032939176 scopus 로고    scopus 로고
    • Solution structure of the 40, 000 Mr phosphoryl transfer complex between the N-terminal domain of enzyme I and HPr
    • Garrett, D. S.; Seok, Y. J.; Peterkofsky, A.; Gronenborn, A. M.; Clore, G. M. Solution structure of the 40, 000 Mr phosphoryl transfer complex between the N-terminal domain of enzyme I and HPr. Nat Struct Biol 1999, 6, 166-173.
    • (1999) Nat Struct Biol , vol.6 , pp. 166-173
    • Garrett, D.S.1    Seok, Y.J.2    Peterkofsky, A.3    Gronenborn, A.M.4    Clore, G.M.5
  • 8
    • 0034792331 scopus 로고    scopus 로고
    • Use of nuclear magnetic resonance to study the three-dimensional structure of rhodopsin
    • Yeagle, P. L.; Albert, A. D. Use of nuclear magnetic resonance to study the three-dimensional structure of rhodopsin. Methods Enzymol 2002, 343, 223-231.
    • (2002) Methods Enzymol , vol.343 , pp. 223-231
    • Yeagle, P.L.1    Albert, A.D.2
  • 9
    • 0034687791 scopus 로고    scopus 로고
    • Synthesis and biophysical analysis of transmembrane domains of a Saccharomyces cerevisiae G protein-coupled receptor
    • Xie, H.; Ding, F. X.; Schreiber, D.; Eng, G.; Liu, S. F.; Arshava, B.; Arevalo, E.; Becker, J. M.; Naider, F. Synthesis and biophysical analysis of transmembrane domains of a Saccharomyces cerevisiae G protein-coupled receptor. Biochemistry 2000, 39, 15462-15474.
    • (2000) Biochemistry , vol.39 , pp. 15462-15474
    • Xie, H.1    Ding, F.X.2    Schreiber, D.3    Eng, G.4    Liu, S.F.5    Arshava, B.6    Arevalo, E.7    Becker, J.M.8    Naider, F.9
  • 10
    • 0037101227 scopus 로고    scopus 로고
    • High-resolution NMR analysis of the seven transmembrane domains of a heptahelical receptor in organic-aqueous medium
    • Arshava, B.; Taran, I.; Xie, H.; Becker, J. M.; Naider, F. High-resolution NMR analysis of the seven transmembrane domains of a heptahelical receptor in organic-aqueous medium. Biopolymers 2002, 64, 161-176.
    • (2002) Biopolymers , vol.64 , pp. 161-176
    • Arshava, B.1    Taran, I.2    Xie, H.3    Becker, J.M.4    Naider, F.5
  • 11
    • 0035745660 scopus 로고    scopus 로고
    • Peptide fragments as models to study the structure of a G-protein coupled receptor: The alpha-factor receptor of Saccharomyces cerevisiae
    • Naider, F.; Arshava, B.; Ding, F. X.; Arevalo, E.; Becker, J. M. Peptide fragments as models to study the structure of a G-protein coupled receptor: The alpha-factor receptor of Saccharomyces cerevisiae. Biopolymers 2001, 60, 334-350.
    • (2001) Biopolymers , vol.60 , pp. 334-350
    • Naider, F.1    Arshava, B.2    Ding, F.X.3    Arevalo, E.4    Becker, J.M.5
  • 12
    • 0035797877 scopus 로고    scopus 로고
    • Studies on the structure of the G-protein-coupled receptor rhodopsin including the putative G-protein binding site in unactivated and activated forms
    • Yeagle, P. L.; Choi, G.; Albert, A. D. Studies on the structure of the G-protein-coupled receptor rhodopsin including the putative G-protein binding site in unactivated and activated forms. Biochemistry 2001, 40, 11932-11937.
    • (2001) Biochemistry , vol.40 , pp. 11932-11937
    • Yeagle, P.L.1    Choi, G.2    Albert, A.D.3
  • 13
    • 0034909370 scopus 로고    scopus 로고
    • Assembly of a polytopic membrane protein structure from the solution structures of overlapping peptide fragments of bacteriorhodopsin
    • Katragadda, M.; Alderfe, R J. L.; Yeagle, P. L. Assembly of a polytopic membrane protein structure from the solution structures of overlapping peptide fragments of bacteriorhodopsin. Biophys J 2001, 81, 1029-1036.
    • (2001) Biophys J , vol.81 , pp. 1029-1036
    • Katragadda, M.1    Alderfe, R.J.L.2    Yeagle, P.L.3
  • 14
    • 0025812324 scopus 로고
    • Model systems for the study of seven-transmem-brane-segment receptors
    • Dohlman, H. G.; Thorner, J.; Caron, M. G.; Lefkowitz, R. J. Model systems for the study of seven-transmem-brane-segment receptors. Annu Rev Biochem 1991, 60, 653-688.
    • (1991) Annu Rev Biochem , vol.60 , pp. 653-688
    • Dohlman, H.G.1    Thorner, J.2    Caron, M.G.3    Lefkowitz, R.J.4
  • 15
    • 0026315381 scopus 로고
    • In vivo topological analysis of Ste2, a yeast plasma membrane protein, by using beta-lactamase gene fusions
    • Cartwright, C. P.; Tipper, D. J. In vivo topological analysis of Ste2, a yeast plasma membrane protein, by using beta-lactamase gene fusions. Mol Cell Biol 1991, 11, 2620-2628.
    • (1991) Mol Cell Biol , vol.11 , pp. 2620-2628
    • Cartwright, C.P.1    Tipper, D.J.2
  • 16
    • 0035979395 scopus 로고    scopus 로고
    • ATR-FTIR study of the structure and orientation of transmembrane domains of the Saccharomyces cerevisiae α-mating factor receptor in phospholipids
    • Ding, F. X.; Xie, H.; Arshava, B.; Becker, J. M.; Naider F. ATR-FTIR study of the structure and orientation of transmembrane domains of the Saccharomyces cerevisiae α-mating factor receptor in phospholipids. Biochemistry 2001, 40, 8945-8954.
    • (2001) Biochemistry , vol.40 , pp. 8945-8954
    • Ding, F.X.1    Xie, H.2    Arshava, B.3    Becker, J.M.4    Naider, F.5
  • 17
    • 0037177850 scopus 로고    scopus 로고
    • The chain length dependence of helix formation of the second transmembrane domain of a G protein-coupled receptor of Saccharomyces cerevisiae
    • Ding, F. X.; Schreiber, D.; VerBerkmoes, N. C.; Becker, J. M.; Naider F. The chain length dependence of helix formation of the second transmembrane domain of a G protein-coupled receptor of Saccharomyces cerevisiae. J Biol Chem 2002, 277, 14483-14492.
    • (2002) J Biol Chem , vol.277 , pp. 14483-14492
    • Ding, F.X.1    Schreiber, D.2    VerBerkmoes, N.C.3    Becker, J.M.4    Naider, F.5
  • 18
    • 0000803035 scopus 로고
    • Polypeptide synthesis using the S-alkyl thioester of a partially protected peptide segment. Synthesis of the DNA-binding domain of c-Myb protein (142-193)-NH2
    • Hojo, A.; Aimoto, S. Polypeptide synthesis using the S-alkyl thioester of a partially protected peptide segment. Synthesis of the DNA-binding domain of c-Myb protein (142-193)-NH2. Bull Chem Soc Jpn 1991, 64, 111-117.
    • (1991) Bull Chem Soc Jpn , vol.64 , pp. 111-117
    • Hojo, A.1    Aimoto, S.2
  • 19
    • 0033553118 scopus 로고    scopus 로고
    • Lactone and lactam library synthesis by silver ion-assisted orthogonal cyclization of unprotected peptides
    • Zhang, L.; Tam, J. P. Lactone and lactam library synthesis by silver ion-assisted orthogonal cyclization of unprotected peptides J Am Chem Soc 1999, 121, 3311-3320.
    • (1999) J Am Chem Soc , vol.121 , pp. 3311-3320
    • Zhang, L.1    Tam, J.P.2
  • 20
    • 0026486811 scopus 로고
    • In situ neutralization in Boc-chemistry solid phase peptide synthesis. Rapid, high yield assembly of difficult sequences
    • Schnolzer, M.; Alewood, P.; Jones, A.; Alewood, D.; Kent S. B. In situ neutralization in Boc-chemistry solid phase peptide synthesis. Rapid, high yield assembly of difficult sequences. Int J Pept Prot Res 1992, 40, 180-193.
    • (1992) Int J Pept Prot Res , vol.40 , pp. 180-193
    • Schnolzer, M.1    Alewood, P.2    Jones, A.3    Alewood, D.4    Kent, S.B.5
  • 21
    • 0030802865 scopus 로고    scopus 로고
    • Preparation of peptide thioesters using Fmoc-solid phase peptide synthesis and its application to the construction of a template assembled synthetic protein (TASP)
    • Futaki, S.; Sogawa, K.; Maruyama, J.; Asahara, T.; Niwa, M. Preparation of peptide thioesters using Fmoc-solid phase peptide synthesis and its application to the construction of a template assembled synthetic protein (TASP). Tetrahedron Lett 1997, 38, 6237-6240.
    • (1997) Tetrahedron Lett , vol.38 , pp. 6237-6240
    • Futaki, S.1    Sogawa, K.2    Maruyama, J.3    Asahara, T.4    Niwa, M.5
  • 23
    • 0033791223 scopus 로고    scopus 로고
    • Synthesis of native proteins by chemical ligation
    • Dawson, P. E.; Kent, S. B. Synthesis of native proteins by chemical ligation. Annu Rev Biochem 2000, 69, 923-960.
    • (2000) Annu Rev Biochem , vol.69 , pp. 923-960
    • Dawson, P.E.1    Kent, S.B.2
  • 24
    • 0035685801 scopus 로고    scopus 로고
    • Methods and strategies of peptide ligation
    • Tam, J. P.; Xu, J.; Eom, K. D. Methods and strategies of peptide ligation. Biopolymers 2001, 60, 194-205.
    • (2001) Biopolymers , vol.60 , pp. 194-205
    • Tam, J.P.1    Xu, J.2    Eom, K.D.3
  • 25
    • 0141670571 scopus 로고    scopus 로고
    • Bio synthesis and biophysical analysis of domains of a yeast G protein-coupled receptor
    • Arevalo, E.; Estephan, R.; Madeo, J.; Arshava, B.; Dumont, M.; Becker, J. M.; Naider, F. Biosynthesis and biophysical analysis of domains of a yeast G protein-coupled receptor. Biopolymer 2003, 71, 516-531.
    • (2003) Biopolymer , vol.71 , pp. 516-531
    • Arevalo, E.1    Estephan, R.2    Madeo, J.3    Arshava, B.4    Dumont, M.5    Becker, J.M.6    Naider, F.7
  • 26
    • 0017873186 scopus 로고
    • Translation of the leader region of the Escherichia coli tryptophan operon
    • Miozzari, G. F.; Yanofsky, C. Translation of the leader region of the Escherichia coli tryptophan operon. J Bacteriol 1978, 133, 1457-1466.
    • (1978) J Bacteriol , vol.133 , pp. 1457-1466
    • Miozzari, G.F.1    Yanofsky, C.2
  • 28
    • 0033547819 scopus 로고    scopus 로고
    • Assembly of G protein-coupled receptors from fragments: Identification of functional receptors with discontinuities in each of the loops connecting transmembrane segments
    • Martin, N. P.; Leavitt, L. M.; Sommers, C. M.; Dumont, M. Assembly of G protein-coupled receptors from fragments: identification of functional receptors with discontinuities in each of the loops connecting transmembrane segments. Biochemistry 1999, 38, 682-695.
    • (1999) Biochemistry , vol.38 , pp. 682-695
    • Martin, N.P.1    Leavitt, L.M.2    Sommers, C.M.3    Dumont, M.4
  • 29
    • 0034992645 scopus 로고    scopus 로고
    • A method for efficient isotopic labeling of recombinant proteins
    • Marley, J.; Lu, M.; Bracken, C. A method for efficient isotopic labeling of recombinant proteins. J Biomol NMR 2001, 20, 71-75.
    • (2001) J Biomol NMR , vol.20 , pp. 71-75
    • Marley, J.1    Lu, M.2    Bracken, C.3
  • 30
    • 0028073893 scopus 로고
    • Formation of a native-like subdomain in a partially folded intermediate of bovine pancreatic trypsin inhibitor
    • Staley, J. P.; Kim, P. S. Formation of a native-like subdomain in a partially folded intermediate of bovine pancreatic trypsin inhibitor. Prot Sci 1994, 3, 1822-1832.
    • (1994) Prot Sci , vol.3 , pp. 1822-1832
    • Staley, J.P.1    Kim, P.S.2
  • 31
    • 0031008165 scopus 로고    scopus 로고
    • Expression and purification of the Saccharomyces cerevisiae α-factor receptor (Ste2p), a 7-transmembrane-segment G protein-coupled receptor
    • David, N. E.; Gee, M.; Andersen, B.; Naider, F.; Thorner, J.; Stevens, R. C. Expression and purification of the Saccharomyces cerevisiae α-factor receptor (Ste2p), a 7-transmembrane-segment G protein-coupled receptor. J Biol Chem 1997, 272, 15553-15561.
    • (1997) J Biol Chem , vol.272 , pp. 15553-15561
    • David, N.E.1    Gee, M.2    Andersen, B.3    Naider, F.4    Thorner, J.5    Stevens, R.C.6
  • 32
    • 0032502747 scopus 로고    scopus 로고
    • Refolding of bacteriorhodopsin from expressed polypeptide fragments
    • Marti, T. Refolding of bacteriorhodopsin from expressed polypeptide fragments. J Biol Chem 1998, 273, 9312-9322.
    • (1998) J Biol Chem , vol.273 , pp. 9312-9322
    • Marti, T.1
  • 33
    • 0036298264 scopus 로고    scopus 로고
    • Mutagenic mapping of helical structures in the transmembrane segments of the yeast α-factor receptor
    • Martin, N. P.; Celic, A.; Dumont, M. E. Mutagenic mapping of helical structures in the transmembrane segments of the yeast α-factor receptor. J Mol Biol 2002, 317, 765-788.
    • (2002) J Mol Biol , vol.317 , pp. 765-788
    • Martin, N.P.1    Celic, A.2    Dumont, M.E.3
  • 35
    • 0033554426 scopus 로고    scopus 로고
    • Total chemical synthesis of the integral membrane protein influenza A virus M2: Role of its C-terminal domain in tetramer assembly
    • Kochendoerfer, G. G.; Salom, D.; Lear, J. D.; Wilk-Orescan, R.; Kent, S. B. DeGrado W. F. Total chemical synthesis of the integral membrane protein influenza A virus M2: Role of its C-terminal domain in tetramer assembly. Biochemistry 1999, 38, 11905-11913.
    • (1999) Biochemistry , vol.38 , pp. 11905-11913
    • Kochendoerfer, G.G.1    Salom, D.2    Lear, J.D.3    Wilk-Orescan, R.4    Kent, S.B.5    DeGrado, W.F.6
  • 36
    • 0033603896 scopus 로고    scopus 로고
    • Engineering and chemical synthesis of a transmembrane protein: The HCV protease cofactor protein NS4A
    • Bianchi, E.; Ingenito, R.; Simon, R. J.; Pessi, A. Engineering and chemical synthesis of a transmembrane protein: The HCV protease cofactor protein NS4A. J Am Chem Soc 1999, 121, 7698-7699.
    • (1999) J Am Chem Soc , vol.121 , pp. 7698-7699
    • Bianchi, E.1    Ingenito, R.2    Simon, R.J.3    Pessi, A.4
  • 37
    • 0037036754 scopus 로고    scopus 로고
    • Semi-synthesis and folding of the potassium channel KcsA
    • Valiyaveetil, F. I.; Mackinnon, R.; Muir, T. W. Semi-synthesis and folding of the potassium channel KcsA. J Am Chem Soc 2002, 124, 9113-9120.
    • (2002) J Am Chem Soc , vol.124 , pp. 9113-9120
    • Valiyaveetil, F.I.1    Mackinnon, R.2    Muir, T.W.3
  • 38
    • 0032499752 scopus 로고    scopus 로고
    • Expressed protein ligation: A general method for protein engineering
    • Muir, T. W.; Sondhi, D.; Col, E. P. A. Expressed protein ligation: A general method for protein engineering. Proc Natl Acad Sci USA 1998, 95, 6705-6710.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 6705-6710
    • Muir, T.W.1    Sondhi, D.2    Col, E.P.A.3


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