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Volumn 106, Issue 28, 2009, Pages 11588-11593

Insertion of short transmembrane helices by the Sec61 translocon

Author keywords

Hydrophobic mismatch; Lipid bilayer; Membrane protein synthesis; Membrane proteins; Molecular dynamics simulation

Indexed keywords

LEUCINE; LYSINE; MEMBRANE PROTEIN; PALMITOYLOLEOYL PHOSPHATIDYLGLYCEROL; PALMITOYLOLEOYL PHOSPHOCHOLINE; PHOSPHATE; PHOSPHATIDYLGLYCEROL; PHOSPHORYLCHOLINE; TRANSLOCON; UNCLASSIFIED DRUG;

EID: 67650869802     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0900638106     Document Type: Article
Times cited : (76)

References (27)
  • 1
    • 0035924329 scopus 로고    scopus 로고
    • Structural basis of water-specific transport through the AQP1 water channel
    • Sui HX, Han B-G, Lee JK, Walian P, Jap BK (2001) Structural basis of water-specific transport through the AQP1 water channel. Nature 414:872-878.
    • (2001) Nature , vol.414 , pp. 872-878
    • Sui, H.X.1    Han, B.-G.2    Lee, J.K.3    Walian, P.4    Jap, B.K.5
  • 2
    • 0037122805 scopus 로고    scopus 로고
    • X-ray structure of a CIC chloride channel at 3.0 Å reveals the molecular basis of anion selectivity
    • Dutzler R, Campbell EB, Cadene M, Chait BT, MacKinnon R (2002) X-ray structure of a CIC chloride channel at 3.0 Å reveals the molecular basis of anion selectivity. Nature 415:287-294.
    • (2002) Nature , vol.415 , pp. 287-294
    • Dutzler, R.1    Campbell, E.B.2    Cadene, M.3    Chait, B.T.4    MacKinnon, R.5
  • 3
    • 0025882870 scopus 로고
    • Systematic analysis of stop-transfer sequence for microsomal membrane
    • Kuroiwa T, Sakaguchi M, Mihara K, Omura T (1991) Systematic analysis of stop-transfer sequence for microsomal membrane. J Biol Chem 266:9251-9255.
    • (1991) J Biol Chem , vol.266 , pp. 9251-9255
    • Kuroiwa, T.1    Sakaguchi, M.2    Mihara, K.3    Omura, T.4
  • 4
    • 0029060799 scopus 로고
    • Artificial transmembrane segments: Requirements for stop transfer and polypeptide orientation
    • Chen H, Kendall DA (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
  • 5
    • 37249037182 scopus 로고    scopus 로고
    • The molecular code for transmembrane-helix recognition by the Sec61 translocon
    • Hessa T, et al. (2007) The molecular code for transmembrane-helix recognition by the Sec61 translocon. Nature 450:1026-1030.
    • (2007) Nature , vol.450 , pp. 1026-1030
    • Hessa, T.1
  • 6
    • 35548971929 scopus 로고    scopus 로고
    • Effect of sequence hydrophobicity and bilayer width upon the minimum length required for the formation of transmembrane helices in membranes
    • Krishnakumar SS, London E (2007) Effect of sequence hydrophobicity and bilayer width upon the minimum length required for the formation of transmembrane helices in membranes. J Mol Biol 374:671-687.
    • (2007) J Mol Biol , vol.374 , pp. 671-687
    • Krishnakumar, S.S.1    London, E.2
  • 7
    • 13444262028 scopus 로고    scopus 로고
    • Recognition of transmembrane helices by the endoplasmic reticulum translocon
    • Hessa T, et al. (2005) Recognition of transmembrane helices by the endoplasmic reticulum translocon. Nature 433:377-381.
    • (2005) Nature , vol.433 , pp. 377-381
    • Hessa, T.1
  • 8
    • 33750498869 scopus 로고    scopus 로고
    • Asn- and Asp-mediated interactions between transmembrane helices during transloconmediated membrane protein assembly
    • Meindl-Beinker NM, Lundin C, Nilsson I, White SH, Von Heijne G (2006) Asn- and Asp-mediated interactions between transmembrane helices during transloconmediated membrane protein assembly. EMBO Rep 7:1111-1116.
    • (2006) EMBO Rep , vol.7 , pp. 1111-1116
    • Meindl-Beinker, N.M.1    Lundin, C.2    Nilsson, I.3    White, S.H.4    Von Heijne, G.5
  • 9
    • 0033516703 scopus 로고    scopus 로고
    • An amphipathic α-helix at a membrane interface: A structural study using a novel X-ray diffraction method
    • Hristova K, et al. (1999) An amphipathic α-helix at a membrane interface: A structural study using a novel X-ray diffraction method. J Mol Biol 290:99-117.
    • (1999) J Mol Biol , vol.290 , pp. 99-117
    • Hristova, K.1
  • 10
    • 0034681908 scopus 로고    scopus 로고
    • Designing transmembrane α-helices that insert spontaneously
    • Wimley WC, White SH (2000) Designing transmembrane α-helices that insert spontaneously. Biochemistry 39:4432-4442.
    • (2000) Biochemistry , vol.39 , pp. 4432-4442
    • Wimley, W.C.1    White, S.H.2
  • 11
    • 0035144532 scopus 로고    scopus 로고
    • Structure, location, and lipid perturbations of melittin at the membrane interface
    • Hristova K, Dempsey CE, White SH (2001) Structure, location, and lipid perturbations of melittin at the membrane interface. Biophys J 80:801-811.
    • (2001) Biophys J , vol.80 , pp. 801-811
    • Hristova, K.1    Dempsey, C.E.2    White, S.H.3
  • 12
    • 1642570286 scopus 로고    scopus 로고
    • Modulation of the bilayer thickness of exocytic pathway membranes by membrane proteins rather than cholesterol
    • Mitra K, Ubarretxena-Belandia I, Taguchi T, Warren G, Engelman DM (2004) Modulation of the bilayer thickness of exocytic pathway membranes by membrane proteins rather than cholesterol. Proc Natl Acad Sci USA 101:4083-4088.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 4083-4088
    • Mitra, K.1    Ubarretxena-Belandia, I.2    Taguchi, T.3    Warren, G.4    Engelman, D.M.5
  • 13
    • 0031980119 scopus 로고    scopus 로고
    • Determination of the hydrocarbon core structure of fluid dioleoylphosphocholine (DOPC) bilayers by X-ray diffraction using specific bromination of the double-bonds: Effect of hydration
    • Hristova K, White SH (1998) Determination of the hydrocarbon core structure of fluid dioleoylphosphocholine (DOPC) bilayers by X-ray diffraction using specific bromination of the double-bonds: Effect of hydration. Biophys J 74:2419-2433.
    • (1998) Biophys J , vol.74 , pp. 2419-2433
    • Hristova, K.1    White, S.H.2
  • 14
    • 0016272524 scopus 로고
    • Membrane proteins: Amino acid sequence and membrane penetration
    • Segrest JP, Feldman RJ (1974) Membrane proteins: Amino acid sequence and membrane penetration. J Mol Biol 87:853-858.
    • (1974) J Mol Biol , vol.87 , pp. 853-858
    • Segrest, J.P.1    Feldman, R.J.2
  • 15
    • 0034284386 scopus 로고    scopus 로고
    • How proteins adapt to a membrane-water interface
    • Killian JA, von Heijne G (2000) How proteins adapt to a membrane-water interface. Trends Biochem Sci 25:429-434.
    • (2000) Trends Biochem Sci , vol.25 , pp. 429-434
    • Killian, J.A.1    von Heijne, G.2
  • 16
    • 7244244196 scopus 로고    scopus 로고
    • Lipids do influence protein function: The hydrophobic matching hypothesis revisited
    • Jensen MØ, Mouritsen OG (2004) Lipids do influence protein function: The hydrophobic matching hypothesis revisited. Biochim Biophys Acta 1666:205-226.
    • (2004) Biochim Biophys Acta , vol.1666 , pp. 205-226
    • Jensen, M.1    Mouritsen, O.G.2
  • 17
    • 0035812599 scopus 로고    scopus 로고
    • Energetics, stability, and prediction of transmembrane helices
    • Jayasinghe S, Hristova K, White SH (2001) Energetics, stability, and prediction of transmembrane helices. J Mol Biol 312:927-934.
    • (2001) J Mol Biol , vol.312 , pp. 927-934
    • Jayasinghe, S.1    Hristova, K.2    White, S.H.3
  • 19
    • 61949084073 scopus 로고    scopus 로고
    • Sequence-specific retention and regulated integration of a nascent membrane protein by the ER Sec61 translocon
    • Pitonzo D, Yang Z, Matsumura Y, Johnson AE, Skach WR (2009) Sequence-specific retention and regulated integration of a nascent membrane protein by the ER Sec61 translocon. Mol Biol Cell 20:685-698.
    • (2009) Mol Biol Cell , vol.20 , pp. 685-698
    • Pitonzo, D.1    Yang, Z.2    Matsumura, Y.3    Johnson, A.E.4    Skach, W.R.5
  • 20
    • 38049074906 scopus 로고    scopus 로고
    • The expanding role of the ER translocon in membrane protein folding
    • Skach WR (2007) The expanding role of the ER translocon in membrane protein folding. J Cell Biol 179:1333-1335.
    • (2007) J Cell Biol , vol.179 , pp. 1333-1335
    • Skach, W.R.1
  • 22
    • 34247614946 scopus 로고    scopus 로고
    • Formation of transmembrane helices in vivo - Is hydrophobicity all that matters?
    • Von HeijneG
    • Von HeijneG(2007) Formation of transmembrane helices in vivo - Is hydrophobicity all that matters? J Gen Physiol 129:353-356.
    • (2007) J Gen Physiol , vol.129 , pp. 353-356
  • 23
    • 34247580102 scopus 로고    scopus 로고
    • Membrane protein insertion: The biology - physics nexus
    • White SH (2007) Membrane protein insertion: The biology - physics nexus. J Gen Physiol 129:363-369.
    • (2007) J Gen Physiol , vol.129 , pp. 363-369
    • White, S.H.1
  • 25
    • 36549093656 scopus 로고
    • Circular dichroism of oriented α helices. I. Proof of the exciton theory
    • Olah GA, Huang HW (1988) Circular dichroism of oriented α helices. I. Proof of the exciton theory. J Chem Phys 89:2531-2538.
    • (1988) J Chem Phys , vol.89 , pp. 2531-2538
    • Olah, G.A.1    Huang, H.W.2
  • 26
    • 0000402127 scopus 로고
    • Circular dichroism of oriented α helices. II. Electric field oriented polypeptides
    • Olah GA, Huang HW (1988) Circular dichroism of oriented α helices. II. Electric field oriented polypeptides. J Chem Phys 89:6956-6962.
    • (1988) J Chem Phys , vol.89 , pp. 6956-6962
    • Olah, G.A.1    Huang, H.W.2
  • 27
    • 0025278431 scopus 로고
    • Method of oriented circular dichroism
    • Wu Y, Huang HW, Olah GA (1990) Method of oriented circular dichroism. Biophys J 57:797-806.
    • (1990) Biophys J , vol.57 , pp. 797-806
    • Wu, Y.1    Huang, H.W.2    Olah, G.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.