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Volumn 46, Issue 51, 2007, Pages 15153-15161

Features of transmembrane segments that promote the lateral release from the translocase into the lipid phase

Author keywords

[No Author keywords available]

Indexed keywords

INTEGRAL MEMBRANE TRANSLOCASES; LIPID PHASES; MEMBRANE INSERTION; TRANSMEMBRANE SEGMENTS;

EID: 37349063087     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi701398y     Document Type: Article
Times cited : (41)

References (40)
  • 1
    • 8844261812 scopus 로고    scopus 로고
    • Sec-translocase mediated membrane protein biogenesis
    • Dalbey, R. E., and Chen, M. (2004) Sec-translocase mediated membrane protein biogenesis, Biochim. Biophys. Acta 1694, 37-53.
    • (2004) Biochim. Biophys. Acta , vol.1694 , pp. 37-53
    • Dalbey, R.E.1    Chen, M.2
  • 3
    • 4644356464 scopus 로고    scopus 로고
    • Membrane-protein integration and the role of the translocation channel
    • Rapoport, T. A., Goder, V., Heinrich, S. U., and Matlack, K. E. (2004) Membrane-protein integration and the role of the translocation channel, Trends Cell Biol. 14, 568-575.
    • (2004) Trends Cell Biol , vol.14 , pp. 568-575
    • Rapoport, T.A.1    Goder, V.2    Heinrich, S.U.3    Matlack, K.E.4
  • 4
    • 33750381048 scopus 로고    scopus 로고
    • The bacterial twin-arginine translocation pathway
    • Lee, P. A., Tullman-Ercek, D., and Georgiou, G. (2006) The bacterial twin-arginine translocation pathway, Annu. Rev. Microbiol. 60, 373-395.
    • (2006) Annu. Rev. Microbiol , vol.60 , pp. 373-395
    • Lee, P.A.1    Tullman-Ercek, D.2    Georgiou, G.3
  • 5
    • 4544233713 scopus 로고    scopus 로고
    • YidC family members are involved in the membrane insertion, lateral integration, folding, and assembly of membrane proteins
    • Dalbey, R. E., and Kuhn, A. (2004) YidC family members are involved in the membrane insertion, lateral integration, folding, and assembly of membrane proteins, J. Cell Biol. 166, 769-774.
    • (2004) J. Cell Biol , vol.166 , pp. 769-774
    • Dalbey, R.E.1    Kuhn, A.2
  • 6
    • 0242439351 scopus 로고    scopus 로고
    • The ribosome and YidC. New insights into the biogenesis of Escherichia coli inner membrane proteins,
    • 4
    • de Gier, J. W., and Luirink, J. (2003) The ribosome and YidC. New insights into the biogenesis of Escherichia coli inner membrane proteins, EMBO Rep. 4, 939-943.
    • (2003) EMBO Rep , pp. 939-943
    • de Gier, J.W.1    Luirink, J.2
  • 7
    • 34047151280 scopus 로고    scopus 로고
    • YidC as an essential and multifunctional component in membrane protein assembly
    • Kiefer, D., and Kuhn, A. (2007) YidC as an essential and multifunctional component in membrane protein assembly, Int. Rev. Cytol. 259, 113-138.
    • (2007) Int. Rev. Cytol , vol.259 , pp. 113-138
    • Kiefer, D.1    Kuhn, A.2
  • 8
    • 15744397061 scopus 로고    scopus 로고
    • YidC - an evolutionary conserved device for the assembly of energy-transducing membrane protein complexes
    • van der Laan, M., Nouwen, N. P., and Driessen, A. J. (2005) YidC - an evolutionary conserved device for the assembly of energy-transducing membrane protein complexes, Curr. Opin. Microbiol. 8, 182-187.
    • (2005) Curr. Opin. Microbiol , vol.8 , pp. 182-187
    • van der Laan, M.1    Nouwen, N.P.2    Driessen, A.J.3
  • 9
    • 0018987976 scopus 로고
    • Intracellular protein topogenesis
    • Blobel, G. (1980) Intracellular protein topogenesis, Proc. Natl. Acad. Sci. U.S.A. 77, 1496-1500.
    • (1980) Proc. Natl. Acad. Sci. U.S.A , vol.77 , pp. 1496-1500
    • Blobel, G.1
  • 10
    • 0018427455 scopus 로고
    • Escherichia coli mutants accumulating the precursor of a secreted protein in the cytoplasm
    • Bassford, P., and Beckwith, J. (1979) Escherichia coli mutants accumulating the precursor of a secreted protein in the cytoplasm, Nature 277, 538-541.
    • (1979) Nature , vol.277 , pp. 538-541
    • Bassford, P.1    Beckwith, J.2
  • 11
    • 0023665037 scopus 로고
    • The internal signal sequence of Escherichia coli leader peptidase is necessary, but not sufficient, for its rapid membrane assembly
    • Dalbey, R. E., Kuhn, A., and Wickner, W. (1987) The internal signal sequence of Escherichia coli leader peptidase is necessary, but not sufficient, for its rapid membrane assembly, J. Biol. Chem. 262, 13241-13245.
    • (1987) J. Biol. Chem , vol.262 , pp. 13241-13245
    • Dalbey, R.E.1    Kuhn, A.2    Wickner, W.3
  • 12
    • 0018236650 scopus 로고
    • Mutations altering the cellular localization of the phage lambda receptor, an Escherichia coli outer membrane protein
    • Emr, S. D., Schwartz, M., and Silhavy, T. J. (1978) Mutations altering the cellular localization of the phage lambda receptor, an Escherichia coli outer membrane protein, Proc. Natl. Acad. Sci. U.S.A. 75, 5802-5806.
    • (1978) Proc. Natl. Acad. Sci. U.S.A , vol.75 , pp. 5802-5806
    • Emr, S.D.1    Schwartz, M.2    Silhavy, T.J.3
  • 13
    • 0022392632 scopus 로고
    • An artificial anchor domain: Hydrophobicity suffices to stop transfer
    • Davis, N. G., and Model, P. (1985) An artificial anchor domain: hydrophobicity suffices to stop transfer, Cell 41, 607-614.
    • (1985) Cell , vol.41 , pp. 607-614
    • Davis, N.G.1    Model, P.2
  • 14
    • 0026516666 scopus 로고
    • Distinct domains of an oligotopic membrane protein are Sec-dependent and Sec-independent for membrane insertion
    • Lee, J. I., Kuhn, A., and Dalbey, R. E. (1992) Distinct domains of an oligotopic membrane protein are Sec-dependent and Sec-independent for membrane insertion, J. Biol. Chem. 267, 938-943.
    • (1992) J. Biol. Chem , vol.267 , pp. 938-943
    • Lee, J.I.1    Kuhn, A.2    Dalbey, R.E.3
  • 15
    • 0023054119 scopus 로고
    • Both hydrophobic domains of M13 procoat are required to initiate membrane insertion
    • Kuhn, A., Kreil, G., and Wickner, W. (1986) Both hydrophobic domains of M13 procoat are required to initiate membrane insertion, EMBO J. 5, 3681-3685.
    • (1986) EMBO J , vol.5 , pp. 3681-3685
    • Kuhn, A.1    Kreil, G.2    Wickner, W.3
  • 16
    • 0025285274 scopus 로고
    • Positively charged residues are important determinants of membrane protein topology
    • Dalbey, R. E. (1990) Positively charged residues are important determinants of membrane protein topology, Trends Biochem. Sci. 15, 253-257.
    • (1990) Trends Biochem. Sci , vol.15 , pp. 253-257
    • Dalbey, R.E.1
  • 17
    • 0025681503 scopus 로고
    • Membrane proteins: From sequence to structure
    • von Heijne, G., and Manoil, C. (1990) Membrane proteins: from sequence to structure, Protein Eng. 4, 109-112.
    • (1990) Protein Eng , vol.4 , pp. 109-112
    • von Heijne, G.1    Manoil, C.2
  • 20
    • 0032515148 scopus 로고    scopus 로고
    • Membrane topology of the 60-kDa Oxa1p homologue from Escherichia coli
    • Saaf, A., Monne, M., de Gier, J. W., and von Heijne, G. (1998) Membrane topology of the 60-kDa Oxa1p homologue from Escherichia coli, J. Biol. Chem. 273, 30415-30418.
    • (1998) J. Biol. Chem , vol.273 , pp. 30415-30418
    • Saaf, A.1    Monne, M.2    de Gier, J.W.3    von Heijne, G.4
  • 21
    • 0034859711 scopus 로고    scopus 로고
    • YidC, an assembly site for polytopic Escherichia coli membrane proteins located in immediate proximity to the SecYE translocon and lipids,
    • 2
    • Beck, K., Eisner, G., Trescher, D., Dalbey, R. E., Brunner, J., and Muller, M. (2001) YidC, an assembly site for polytopic Escherichia coli membrane proteins located in immediate proximity to the SecYE translocon and lipids, EMBO Rep. 2, 709-714.
    • (2001) EMBO Rep , pp. 709-714
    • Beck, K.1    Eisner, G.2    Trescher, D.3    Dalbey, R.E.4    Brunner, J.5    Muller, M.6
  • 22
    • 0037040894 scopus 로고    scopus 로고
    • Direct interaction of YidC with the Sec-independent Pf3 coat protein during its membrane protein insertion
    • Chen, M., Samuelson, J. C., Jiang, F., Muller, M., Kuhn, A., and Dalbey, R. E. (2002) Direct interaction of YidC with the Sec-independent Pf3 coat protein during its membrane protein insertion, J. Biol. Chem. 277, 7670-7675.
    • (2002) J. Biol. Chem , vol.277 , pp. 7670-7675
    • Chen, M.1    Samuelson, J.C.2    Jiang, F.3    Muller, M.4    Kuhn, A.5    Dalbey, R.E.6
  • 23
    • 0034617438 scopus 로고    scopus 로고
    • Nascent Lep inserts into the Escherichia coli inner membrane in the vicinity of YidC, SecY and SecA
    • Houben, E. N., Scotti, P. A., Valent, Q. A., Brunner, J., de Gier, J. L., Oudega, B., and Luirink, J. (2000) Nascent Lep inserts into the Escherichia coli inner membrane in the vicinity of YidC, SecY and SecA, FEBS Lett. 476, 229-233.
    • (2000) FEBS Lett , vol.476 , pp. 229-233
    • Houben, E.N.1    Scotti, P.A.2    Valent, Q.A.3    Brunner, J.4    de Gier, J.L.5    Oudega, B.6    Luirink, J.7
  • 26
    • 0035854694 scopus 로고    scopus 로고
    • YidC/Oxa1p/Alb3: Evolutionarily conserved mediators of membrane protein assembly
    • Luirink, J., Samuelsson, T., and de Gier, J. W. (2001) YidC/Oxa1p/Alb3: evolutionarily conserved mediators of membrane protein assembly, FEBS Lett. 501, 1-5.
    • (2001) FEBS Lett , vol.501 , pp. 1-5
    • Luirink, J.1    Samuelsson, T.2    de Gier, J.W.3
  • 27
    • 0035856567 scopus 로고    scopus 로고
    • Phylogenetic and structural analyses of the oxal family of protein translocases
    • Yen, M. R., Harley, K. T., Tseng, Y. H., and Saier, M. H., Jr. (2001) Phylogenetic and structural analyses of the oxal family of protein translocases, FEMS Microbiol. Lett. 204, 223-231.
    • (2001) FEMS Microbiol. Lett , vol.204 , pp. 223-231
    • Yen, M.R.1    Harley, K.T.2    Tseng, Y.H.3    Saier Jr., M.H.4
  • 28
    • 1542676909 scopus 로고    scopus 로고
    • Defining the regions of Escherichia coli YidC that contribute to activity
    • Jiang, F., Chen, M., Yi, L., de Gier, J. W., Kuhn, A., and Dalbey, R. E. (2003) Defining the regions of Escherichia coli YidC that contribute to activity, J. Biol. Chem. 278, 48965-48972.
    • (2003) J. Biol. Chem , vol.278 , pp. 48965-48972
    • Jiang, F.1    Chen, M.2    Yi, L.3    de Gier, J.W.4    Kuhn, A.5    Dalbey, R.E.6
  • 29
    • 0025675488 scopus 로고
    • The function of a leader peptide in translocating charged amino acyl residues across a membrane
    • Rohrer, J., and Kuhn, A. (1990) The function of a leader peptide in translocating charged amino acyl residues across a membrane, Science 250, 1418-1421.
    • (1990) Science , vol.250 , pp. 1418-1421
    • Rohrer, J.1    Kuhn, A.2
  • 30
    • 4544234959 scopus 로고    scopus 로고
    • Sec/SRP requirements and energetics of membrane insertion of subunits a, b, and c of the Escherichia coli F1F0 ATP synthase
    • Yi, L., Celebi, N., Chen, M., and Dalbey, R. E. (2004) Sec/SRP requirements and energetics of membrane insertion of subunits a, b, and c of the Escherichia coli F1F0 ATP synthase, J. Biol. Chem. 279, 39260-39267.
    • (2004) J. Biol. Chem , vol.279 , pp. 39260-39267
    • Yi, L.1    Celebi, N.2    Chen, M.3    Dalbey, R.E.4
  • 31
    • 1842611517 scopus 로고    scopus 로고
    • Rapp, M., Drew, D., Daley, D. O., Nilsson, J., Carvalho, T., Melen, K., De, Gier, J. W., and Von, Heijne, G. (2004) Experimentally based topology models for E. coli inner membrane proteins, Protein Sci. 13, 937-945.
    • Rapp, M., Drew, D., Daley, D. O., Nilsson, J., Carvalho, T., Melen, K., De, Gier, J. W., and Von, Heijne, G. (2004) Experimentally based topology models for E. coli inner membrane proteins, Protein Sci. 13, 937-945.
  • 32
    • 0029017155 scopus 로고
    • Escherichia coli alkaline phosphatase localized to the cytoplasm slowly acquires enzymatic activity in cells whose growth has been suspended: A caution for gene fusion studies
    • Derman, A. I., and Beckwith, J. (1995) Escherichia coli alkaline phosphatase localized to the cytoplasm slowly acquires enzymatic activity in cells whose growth has been suspended: a caution for gene fusion studies, J. Bacteriol. 177, 3764-3770.
    • (1995) J. Bacteriol , vol.177 , pp. 3764-3770
    • Derman, A.I.1    Beckwith, J.2
  • 33
    • 0026047004 scopus 로고
    • Analysis of membrane protein topology using alkaline phosphatase and beta-galactosidase gene fusions
    • Manoil, C. (1991) Analysis of membrane protein topology using alkaline phosphatase and beta-galactosidase gene fusions, Methods Cell Biol. 34, 61-75.
    • (1991) Methods Cell Biol , vol.34 , pp. 61-75
    • Manoil, C.1
  • 34
    • 0028935007 scopus 로고
    • The translocation of negatively charged residues across the membrane is driven by the electrochemical potential: Evidence for an electrophoresis-like membrane transfer mechanism
    • Cao, G., Kuhn, A., and Dalbey, R. E. (1995) The translocation of negatively charged residues across the membrane is driven by the electrochemical potential: evidence for an electrophoresis-like membrane transfer mechanism, EMBO J. 14, 866-875.
    • (1995) EMBO J , vol.14 , pp. 866-875
    • Cao, G.1    Kuhn, A.2    Dalbey, R.E.3
  • 35
    • 0022967093 scopus 로고
    • The role of the polar, carboxyl-terminal domain of Escherichia coli leader peptidase in its translocation across the plasma membrane
    • Dalbey, R. E., and Wickner, W. (1986) The role of the polar, carboxyl-terminal domain of Escherichia coli leader peptidase in its translocation across the plasma membrane, J. Biol. Chem. 261, 13844-13849.
    • (1986) J. Biol. Chem , vol.261 , pp. 13844-13849
    • Dalbey, R.E.1    Wickner, W.2
  • 36
    • 0025087137 scopus 로고
    • Azide-resistant mutants of Escherichia coli alter the SecA protein, an azide-sensitive component of the protein export machinery
    • Oliver, D. B., Cabelli, R. J., Dolan, K. M., and Jarosik, G. P. (1990) Azide-resistant mutants of Escherichia coli alter the SecA protein, an azide-sensitive component of the protein export machinery, Proc. Natl. Acad. Sci. U.S.A. 87, 8227-8231.
    • (1990) Proc. Natl. Acad. Sci. U.S.A , vol.87 , pp. 8227-8231
    • Oliver, D.B.1    Cabelli, R.J.2    Dolan, K.M.3    Jarosik, G.P.4
  • 37
    • 0025277448 scopus 로고    scopus 로고
    • Kuhn, A., Zhu, H. Y., and Dalbey, R. E. (1990) Efficient translocation of positively charged residues of M13 procoat protein across the membrane excludes electrophoresis as the primary force for membrane insertion [published erratum: (1990) EMBO J. 9 (10), 3413], EMBO J. 9, 2385-2388, 2429.
    • Kuhn, A., Zhu, H. Y., and Dalbey, R. E. (1990) Efficient translocation of positively charged residues of M13 procoat protein across the membrane excludes electrophoresis as the primary force for membrane insertion [published erratum: (1990) EMBO J. 9 (10), 3413], EMBO J. 9, 2385-2388, 2429.
  • 38
    • 20044389842 scopus 로고    scopus 로고
    • Membrane insertion of a potassium-channel voltage sensor
    • Hessa, T., White, S. H., and von Heijne, G. (2005) Membrane insertion of a potassium-channel voltage sensor, Science 307, 1427.
    • (2005) Science , vol.307 , pp. 1427
    • Hessa, T.1    White, S.H.2    von Heijne, G.3
  • 39
    • 0023028051 scopus 로고
    • A genetic approach to analyzing membrane protein topology
    • Manoil, C., and Beckwith, J. (1986) A genetic approach to analyzing membrane protein topology, Science 233, 1403-1408.
    • (1986) Science , vol.233 , pp. 1403-1408
    • Manoil, C.1    Beckwith, J.2
  • 40
    • 0029060799 scopus 로고
    • Artificial transmembrane segments. Requirements for stop transfer and polypeptide orientation
    • Chen, H., and Kendall, D. A. (1995) Artificial transmembrane segments. Requirements for stop transfer and polypeptide orientation, J. Biol. Chem. 270, 14115-14122.
    • (1995) J. Biol. Chem , vol.270 , pp. 14115-14122
    • Chen, H.1    Kendall, D.A.2


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