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Volumn 49, Issue 2, 2010, Pages 279-286

A single glutamate residue controls the oligomerization, function, and stability of the aquaglyceroporin GlpF

Author keywords

[No Author keywords available]

Indexed keywords

CELLULAR MEMBRANES; CHANNEL FUNCTIONS; E. COLI; HELICAL MEMBRANE; HIGHER ORDER; IN-VITRO; IN-VIVO; OLIGOMERIC STATE; OLIGOMERIC STRUCTURE; POLAR RESIDUES; POTENTIAL IMPACTS; PROTEIN FUNCTIONS;

EID: 75349084208     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi901660t     Document Type: Article
Times cited : (29)

References (53)
  • 1
    • 0031954925 scopus 로고    scopus 로고
    • Genome-wide analysis of integral membrane proteins from eubacterial, archaean, and eukaryotic organisms
    • Wallin, E., and von Heijne, G. (1998) Genome-wide analysis of integral membrane proteins from eubacterial, archaean, and eukaryotic organisms. Protein Sci. 7, 1029-1038.
    • (1998) Protein Sci , vol.7 , pp. 1029-1038
    • Wallin, E.1    von Heijne, G.2
  • 2
    • 28444488355 scopus 로고    scopus 로고
    • Solving the membrane protein folding problem
    • Bowie, J. U. (2005) Solving the membrane protein folding problem. Nature 438, 581-589.
    • (2005) Nature , vol.438 , pp. 581-589
    • Bowie, J.U.1
  • 3
    • 60349125439 scopus 로고    scopus 로고
    • Folding scene investigation: Membrane proteins
    • Booth, P. J., and Curnow, P. (2009) Folding scene investigation: Membrane proteins. Curr. Opin. Struct. Biol. 19, 8-13.
    • (2009) Curr. Opin. Struct. Biol , vol.19 , pp. 8-13
    • Booth, P.J.1    Curnow, P.2
  • 4
    • 46049088691 scopus 로고    scopus 로고
    • Proteinprotein interactions in the membrane: Sequence, structural, and biological motifs
    • Moore, D. T., Berger, B. W., and DeGrado, W. F. (2008) Proteinprotein interactions in the membrane: Sequence, structural, and biological motifs. Structure 16, 991-1001.
    • (2008) Structure , vol.16 , pp. 991-1001
    • Moore, D.T.1    Berger, B.W.2    DeGrado, W.F.3
  • 5
    • 0033790343 scopus 로고    scopus 로고
    • Helical membrane protein folding, stability, and evolution
    • Popot, J. L., and Engelman, D. M. (2000) Helical membrane protein folding, stability, and evolution. Annu. Rev. Biochem. 69, 881-922.
    • (2000) Annu. Rev. Biochem , vol.69 , pp. 881-922
    • Popot, J.L.1    Engelman, D.M.2
  • 6
    • 0025249842 scopus 로고
    • Membrane protein folding and oligomerization: The two-stage model
    • Popot, J. L., and Engelman, D.M. (1990) Membrane protein folding and oligomerization: The two-stage model. Biochemistry 29, 4031-4037.
    • (1990) Biochemistry , vol.29 , pp. 4031-4037
    • Popot, J.L.1    Engelman, D.M.2
  • 7
    • 14544300522 scopus 로고    scopus 로고
    • CFTR channel opening by ATP-driven tight dimerization of its nucleotide-binding domains
    • Vergani, P., Lockless, S. W., Nairn, A. C., and Gadsby, D. C. (2005) CFTR channel opening by ATP-driven tight dimerization of its nucleotide-binding domains. Nature 433, 876-880.
    • (2005) Nature , vol.433 , pp. 876-880
    • Vergani, P.1    Lockless, S.W.2    Nairn, A.C.3    Gadsby, D.C.4
  • 8
    • 34250666273 scopus 로고    scopus 로고
    • A monomeric G protein-coupled receptor isolated in a high-density lipoprotein particle efficiently activates itsGprotein
    • Whorton, M. R., Bokoch, M. P., Rasmussen, S. G., Huang, B., Zare, R. N., Kobilka, B., and Sunahara, R. K. (2007) A monomeric G protein-coupled receptor isolated in a high-density lipoprotein particle efficiently activates itsGprotein. Proc. Natl. Acad. Sci. U.S.A. 104, 7682-7687.
    • (2007) Proc. Natl. Acad. Sci. U.S.A , vol.104 , pp. 7682-7687
    • Whorton, M.R.1    Bokoch, M.P.2    Rasmussen, S.G.3    Huang, B.4    Zare, R.N.5    Kobilka, B.6    Sunahara, R.K.7
  • 9
    • 33947369500 scopus 로고    scopus 로고
    • G protein-coupled receptor dimerisation: Molecular basis and relevance to function
    • Milligan, G. (2007) G protein-coupled receptor dimerisation: Molecular basis and relevance to function. Biochim. Biophys. Acta 1768, 825-835.
    • (2007) Biochim. Biophys. Acta , vol.1768 , pp. 825-835
    • Milligan, G.1
  • 11
    • 33748602095 scopus 로고    scopus 로고
    • Molecular mechanisms of aquaporin biogenesis by the endoplasmic reticulum Sec61 translocon
    • Pitonzo, D., and Skach, W. R. (2006) Molecular mechanisms of aquaporin biogenesis by the endoplasmic reticulum Sec61 translocon. Biochim. Biophys. Acta 1758, 976-988.
    • (2006) Biochim. Biophys. Acta , vol.1758 , pp. 976-988
    • Pitonzo, D.1    Skach, W.R.2
  • 12
    • 66849131417 scopus 로고    scopus 로고
    • Cellular mechanisms of membrane protein folding
    • Skach, W. R. (2009) Cellular mechanisms of membrane protein folding. Nat. Struct. Mol. Biol. 16, 606-612.
    • (2009) Nat. Struct. Mol. Biol , vol.16 , pp. 606-612
    • Skach, W.R.1
  • 13
    • 34547650465 scopus 로고    scopus 로고
    • A novel tripartite motif involved in aquaporin topogenesis, monomer folding and tetramerization
    • Buck, T. M., Wagner, J., Grund, S., and Skach, W. R. (2007) A novel tripartite motif involved in aquaporin topogenesis, monomer folding and tetramerization. Nat. Struct. Mol. Biol. 14, 762-769.
    • (2007) Nat. Struct. Mol. Biol , vol.14 , pp. 762-769
    • Buck, T.M.1    Wagner, J.2    Grund, S.3    Skach, W.R.4
  • 14
    • 23044496908 scopus 로고    scopus 로고
    • What Makes an Aquaporin a Glycerol Channel? A Comparative Study of AqpZ and GlpF
    • Wang, Y., Schulten, K., and Tajkhorshid, E. (2005) What Makes an Aquaporin a Glycerol Channel? A Comparative Study of AqpZ and GlpF. Structure 13, 1107-1118.
    • (2005) Structure , vol.13 , pp. 1107-1118
    • Wang, Y.1    Schulten, K.2    Tajkhorshid, E.3
  • 15
    • 85177145597 scopus 로고    scopus 로고
    • Maurel, C., Reizer, J., Schroeder, J. I., Chrispeels, M. J., and Saier, M. H., Jr. (1994) Functional characterization of the Escherichia coli glycerol facilitator, GlpF, in Xenopus oocytes. J. Biol. Chem. 269, 11869-11872.
    • Maurel, C., Reizer, J., Schroeder, J. I., Chrispeels, M. J., and Saier, M. H., Jr. (1994) Functional characterization of the Escherichia coli glycerol facilitator, GlpF, in Xenopus oocytes. J. Biol. Chem. 269, 11869-11872.
  • 16
    • 0030953720 scopus 로고    scopus 로고
    • Antimonite is accumulated by the glycerol facilitator GlpF in Escherichia coli
    • Sanders, O. I., Rensing, C., Kuroda, M., Mitra, B., and Rosen, B. P. (1997) Antimonite is accumulated by the glycerol facilitator GlpF in Escherichia coli. J. Bacteriol. 179, 3365-3367.
    • (1997) J. Bacteriol , vol.179 , pp. 3365-3367
    • Sanders, O.I.1    Rensing, C.2    Kuroda, M.3    Mitra, B.4    Rosen, B.P.5
  • 17
    • 0027410583 scopus 로고
    • Glycerol kinase of Escherichia coli is activated by interaction with the glycerol facilitator
    • Voegele, R. T., Sweet, G. D., and Boos, W. (1993) Glycerol kinase of Escherichia coli is activated by interaction with the glycerol facilitator. J. Bacteriol. 175, 1087-1094.
    • (1993) J. Bacteriol , vol.175 , pp. 1087-1094
    • Voegele, R.T.1    Sweet, G.D.2    Boos, W.3
  • 19
    • 33644850534 scopus 로고    scopus 로고
    • Crystal structure of AqpZ tetramer reveals two distinct Arg-189 conformations associated with water permeation through the narrowest constriction of the waterconducting channel
    • Jiang, J., Daniels, B. V., and Fu, D. (2006) Crystal structure of AqpZ tetramer reveals two distinct Arg-189 conformations associated with water permeation through the narrowest constriction of the waterconducting channel. J. Biol. Chem. 281, 454-460.
    • (2006) J. Biol. Chem , vol.281 , pp. 454-460
    • Jiang, J.1    Daniels, B.V.2    Fu, D.3
  • 21
    • 0035956936 scopus 로고    scopus 로고
    • Reconstitution and functional comparison of purifiedGlpF and AqpZ, the glycerol and water channels from Escherichia coli
    • Borgnia, M. J., and Agre, P. (2001) Reconstitution and functional comparison of purifiedGlpF and AqpZ, the glycerol and water channels from Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 98, 2888-2893.
    • (2001) Proc. Natl. Acad. Sci. U.S.A , vol.98 , pp. 2888-2893
    • Borgnia, M.J.1    Agre, P.2
  • 23
    • 0036209785 scopus 로고    scopus 로고
    • Aquaglyceroporins: Channel proteins with a conserved core, multiple functions, and variable surfaces
    • Engel, A., and Stahlberg, H. (2002) Aquaglyceroporins: Channel proteins with a conserved core, multiple functions, and variable surfaces. Int. Rev. Cytol. 215, 75-104.
    • (2002) Int. Rev. Cytol , vol.215 , pp. 75-104
    • Engel, A.1    Stahlberg, H.2
  • 25
    • 67649963000 scopus 로고    scopus 로고
    • Fischer, G., Kosinska-Eriksson, U., Aponte-Santamaria, C., Palmgren, M., Geijer, C., Hedfalk, K.,Hohmann, S., de Groot, B. L.,Neutze, R., and Lindkvist-Petersson,K. (2009) Crystal structure of a yeast aquaporin at 1.15 angstrom reveals a novel gating mechanism. PLoS Biol. 7, e1000130.
    • Fischer, G., Kosinska-Eriksson, U., Aponte-Santamaria, C., Palmgren, M., Geijer, C., Hedfalk, K.,Hohmann, S., de Groot, B. L.,Neutze, R., and Lindkvist-Petersson,K. (2009) Crystal structure of a yeast aquaporin at 1.15 angstrom reveals a novel gating mechanism. PLoS Biol. 7, e1000130.
  • 26
    • 0007949690 scopus 로고    scopus 로고
    • Interhelical hydrogen bonding drives strong interactions in membrane proteins
    • Zhou, F. X., Cocco,M. J., Russ,W. P., Brunger, A. T., and Engelman, D. M. (2000) Interhelical hydrogen bonding drives strong interactions in membrane proteins. Nat. Struct. Biol. 7, 154-160.
    • (2000) Nat. Struct. Biol , vol.7 , pp. 154-160
    • Zhou, F.X.1    Cocco, M.J.2    Russ, W.P.3    Brunger, A.T.4    Engelman, D.M.5
  • 28
    • 0035969998 scopus 로고    scopus 로고
    • Polar side chains drive the association of model transmembrane peptides
    • Gratkowski, H., Lear, J. D., and DeGrado, W. F. (2001) Polar side chains drive the association of model transmembrane peptides. Proc. Natl. Acad. Sci. U.S.A. 98, 880-885.
    • (2001) Proc. Natl. Acad. Sci. U.S.A , vol.98 , pp. 880-885
    • Gratkowski, H.1    Lear, J.D.2    DeGrado, W.F.3
  • 29
    • 0034952420 scopus 로고    scopus 로고
    • Interhelical hydrogen bonds in the CFTR membrane domain
    • Therien, A. G., Grant, F. E., and Deber, C. M. (2001) Interhelical hydrogen bonds in the CFTR membrane domain. Nat. Struct. Biol. 8, 597-601.
    • (2001) Nat. Struct. Biol , vol.8 , pp. 597-601
    • Therien, A.G.1    Grant, F.E.2    Deber, C.M.3
  • 31
    • 0037474296 scopus 로고    scopus 로고
    • GALLEX, a Measurement of Heterologous Association of Transmembrane Helices in a Biological Membrane
    • Schneider, D., and Engelman, D. M. (2003) GALLEX, a Measurement of Heterologous Association of Transmembrane Helices in a Biological Membrane. J. Biol. Chem. 278, 3105-3111.
    • (2003) J. Biol. Chem , vol.278 , pp. 3105-3111
    • Schneider, D.1    Engelman, D.M.2
  • 33
    • 25144470713 scopus 로고    scopus 로고
    • Pore selectivity analysis of an aquaglyceroporin by stopped-flow spectrophotometry on bacterial cell suspensions
    • Hubert, J. F., Duchesne, L., Delamarche, C., Vaysse, A., Gueune, H., and Raguenes-Nicol, C. (2005) Pore selectivity analysis of an aquaglyceroporin by stopped-flow spectrophotometry on bacterial cell suspensions. Biol. Cell 97, 675-686.
    • (2005) Biol. Cell , vol.97 , pp. 675-686
    • Hubert, J.F.1    Duchesne, L.2    Delamarche, C.3    Vaysse, A.4    Gueune, H.5    Raguenes-Nicol, C.6
  • 34
    • 0033547240 scopus 로고    scopus 로고
    • Rapid gating and anion permeability of an intracellular aquaporin
    • Yasui, M., Hazama, A., Kwon, T. H., Nielsen, S., Guggino, W. B., and Agre, P. (1999) Rapid gating and anion permeability of an intracellular aquaporin. Nature 402, 184-187.
    • (1999) Nature , vol.402 , pp. 184-187
    • Yasui, M.1    Hazama, A.2    Kwon, T.H.3    Nielsen, S.4    Guggino, W.B.5    Agre, P.6
  • 36
  • 37
    • 20544459748 scopus 로고    scopus 로고
    • Defining the structural basis for assembly of a transmembrane cytochrome
    • Prodöhl, A., Volkmer, T., Finger, C., and Schneider, D. (2005) Defining the structural basis for assembly of a transmembrane cytochrome. J. Mol. Biol. 350, 744-756.
    • (2005) J. Mol. Biol , vol.350 , pp. 744-756
    • Prodöhl, A.1    Volkmer, T.2    Finger, C.3    Schneider, D.4
  • 38
    • 0037133518 scopus 로고    scopus 로고
    • Polar residues in membrane domains of proteins: Molecular basis for helixhelix association in a mutant CFTR transmembrane segment
    • Partridge, A. W., Melnyk, R. A., and Deber, C. M. (2002) Polar residues in membrane domains of proteins: Molecular basis for helixhelix association in a mutant CFTR transmembrane segment. Biochemistry 41, 3647-3653.
    • (2002) Biochemistry , vol.41 , pp. 3647-3653
    • Partridge, A.W.1    Melnyk, R.A.2    Deber, C.M.3
  • 39
  • 40
    • 65549101578 scopus 로고    scopus 로고
    • Polar residues in transmembrane helices can decrease electrophoretic mobility in polyacrylamide gels without causing helix dimerization
    • Walkenhorst, W. F., Merzlyakov, M., Hristova, K., and Wimley, W. C. (2009) Polar residues in transmembrane helices can decrease electrophoretic mobility in polyacrylamide gels without causing helix dimerization. Biochim. Biophys. Acta 1788, 1321-1331.
    • (2009) Biochim. Biophys. Acta , vol.1788 , pp. 1321-1331
    • Walkenhorst, W.F.1    Merzlyakov, M.2    Hristova, K.3    Wimley, W.C.4
  • 41
    • 35248840065 scopus 로고    scopus 로고
    • A mutational study of transmembrane helix-helix interactions
    • Prodöhl, A., Weber, M., Dreher, C., and Schneider, D. (2007) A mutational study of transmembrane helix-helix interactions. Biochimie 89, 1433-1437.
    • (2007) Biochimie , vol.89 , pp. 1433-1437
    • Prodöhl, A.1    Weber, M.2    Dreher, C.3    Schneider, D.4
  • 42
    • 33847270649 scopus 로고    scopus 로고
    • From Interactions of Single Transmembrane Helices to Folding of α-Helical Membrane Proteins: Analyzing Transmembrane Helix-Helix Interactions in Bacteria
    • Schneider, D., Finger, C., Prodöhl, A., and Volkmer, T. (2007) From Interactions of Single Transmembrane Helices to Folding of α-Helical Membrane Proteins: Analyzing Transmembrane Helix-Helix Interactions in Bacteria. Curr. Protein Pept. Sci. 8, 45-61.
    • (2007) Curr. Protein Pept. Sci , vol.8 , pp. 45-61
    • Schneider, D.1    Finger, C.2    Prodöhl, A.3    Volkmer, T.4
  • 43
    • 33646078118 scopus 로고    scopus 로고
    • The stability of transmembrane helix interactions measured in a biological membrane
    • Finger, C., Volkmer, T., Prodöhl, A., Otzen, D. E., Engelman, D. M., and Schneider, D. (2006) The stability of transmembrane helix interactions measured in a biological membrane. J. Mol. Biol. 358, 1221-1228.
    • (2006) J. Mol. Biol , vol.358 , pp. 1221-1228
    • Finger, C.1    Volkmer, T.2    Prodöhl, A.3    Otzen, D.E.4    Engelman, D.M.5    Schneider, D.6
  • 47
    • 41149127245 scopus 로고    scopus 로고
    • Vertebrate membrane proteins: Structure, function, and insights from biophysical approaches
    • Muller, D. J., Wu, N., and Palczewski, K. (2008) Vertebrate membrane proteins: Structure, function, and insights from biophysical approaches. Pharmacol. Rev. 60, 43-78.
    • (2008) Pharmacol. Rev , vol.60 , pp. 43-78
    • Muller, D.J.1    Wu, N.2    Palczewski, K.3
  • 48
    • 29144532994 scopus 로고    scopus 로고
    • Characterizing molecular interactions in different bacteriorhodopsin assemblies by single-molecule force spectroscopy
    • Sapra, K. T., Besir, H., Oesterhelt, D., and Muller, D. J. (2006) Characterizing molecular interactions in different bacteriorhodopsin assemblies by single-molecule force spectroscopy. J. Mol. Biol. 355, 640-650.
    • (2006) J. Mol. Biol , vol.355 , pp. 640-650
    • Sapra, K.T.1    Besir, H.2    Oesterhelt, D.3    Muller, D.J.4
  • 49
    • 33744939757 scopus 로고    scopus 로고
    • Mitochondrial membrane potential is dependent on the oligomeric state of F1F0-ATP synthase supracomplexes
    • Bornhovd, C., Vogel, F., Neupert, W., and Reichert, A. S. (2006) Mitochondrial membrane potential is dependent on the oligomeric state of F1F0-ATP synthase supracomplexes. J. Biol. Chem. 281, 13990-13998.
    • (2006) J. Biol. Chem , vol.281 , pp. 13990-13998
    • Bornhovd, C.1    Vogel, F.2    Neupert, W.3    Reichert, A.S.4
  • 51
    • 39149104024 scopus 로고    scopus 로고
    • GPCR monomers and oligomers: It takes all kinds
    • Gurevich, V. V., and Gurevich, E. V. (2008) GPCR monomers and oligomers: It takes all kinds. Trends Neurosci. 31, 74-81.
    • (2008) Trends Neurosci , vol.31 , pp. 74-81
    • Gurevich, V.V.1    Gurevich, E.V.2
  • 52
    • 0033546303 scopus 로고    scopus 로고
    • Oligomerization state influences the degradation rate of 3-hydroxy-3- methylglutaryl-CoA reductase
    • Cheng, H. H., Xu, L., Kumagai, H., and Simoni, R. D. (1999) Oligomerization state influences the degradation rate of 3-hydroxy-3- methylglutaryl-CoA reductase. J. Biol. Chem. 274, 17171-17178.
    • (1999) J. Biol. Chem , vol.274 , pp. 17171-17178
    • Cheng, H.H.1    Xu, L.2    Kumagai, H.3    Simoni, R.D.4
  • 53
    • 0028555357 scopus 로고
    • Use of the tetracycline promoter for the tightly regulated production of a murine antibody fragment in Escherichia coli
    • Skerra, A. (1994) Use of the tetracycline promoter for the tightly regulated production of a murine antibody fragment in Escherichia coli. Gene 151, 131-135.
    • (1994) Gene , vol.151 , pp. 131-135
    • Skerra, A.1


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