메뉴 건너뛰기




Volumn 107, Issue 40, 2010, Pages 17182-17187

Lateral opening of a translocon upon entry of protein suggests the mechanism of insertion into membranes

Author keywords

Membrane protein folding; Nascent protein chain; Secretion; Translocation

Indexed keywords

CHAPERONE; TRANSLOCON;

EID: 78049253482     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1012556107     Document Type: Article
Times cited : (145)

References (40)
  • 1
    • 4143101547 scopus 로고    scopus 로고
    • The machinery of membrane protein assembly
    • White SH, von Heijne G (2004) The machinery of membrane protein assembly. Curr Opin Struct Biol 14:397-404.
    • (2004) Curr Opin Struct Biol , vol.14 , pp. 397-404
    • White, S.H.1    Von Heijne, G.2
  • 2
    • 0025087853 scopus 로고
    • The purified E. coli integral membrane protein SecY/E is sufficient for reconstitution of SecA-dependent precursor protein translocation
    • DOI 10.1016/0092-8674(90)90111-Q
    • Brundage L, Hendrick JP, Schiebel E, Driessen AJ, WicknerW(1990) The purified E. coli integral membrane protein SecY/E is sufficient for reconstitution of SecA-dependent precursor protein translocation. Cell 62:649-657. (Pubitemid 20275706)
    • (1990) Cell , vol.62 , Issue.4 , pp. 649-657
    • Brundage, L.1    Hendrick, J.P.2    Schiebel, E.3    Driessen, A.J.M.4    Wickner, W.5
  • 3
    • 0345196631 scopus 로고    scopus 로고
    • The bacterial SecY/E translocation complex forms channel-like structures similar to those of the eukaryotic Sec61p complex
    • Meyer TH, et al. (1999) The bacterial SecY/E translocation complex forms channel-like structures similar to those of the eukaryotic Sec61p complex. J Mol Biol 285:1789-1800.
    • (1999) J Mol Biol , vol.285 , pp. 1789-1800
    • Meyer, T.H.1
  • 4
    • 17044419154 scopus 로고    scopus 로고
    • Targeting proteins to membranes: Structure of the signal recognition particle
    • DOI 10.1016/j.sbi.2005.03.007, Theory and Simulation/Macromolecular Assemblages
    • Egea PF, Stroud RM, Walter P (2005) Targeting proteins to membranes: Structure of the signal recognition particle. Curr Opin Struct Biol 15:213-220. (Pubitemid 40503343)
    • (2005) Current Opinion in Structural Biology , vol.15 , Issue.2 , pp. 213-220
    • Egea, P.F.1    Stroud, R.M.2    Walter, P.3
  • 5
    • 34548206622 scopus 로고    scopus 로고
    • Interactions that drive Sec-dependent bacterial protein transport
    • Rusch SL, Kendall DA (2007) Interactions that drive Sec-dependent bacterial protein transport. Biochemistry 46:9665-9673.
    • (2007) Biochemistry , vol.46 , pp. 9665-9673
    • Rusch, S.L.1    Kendall, D.A.2
  • 6
    • 0347087516 scopus 로고    scopus 로고
    • SecYEG Proteoliposomes Catalyze the Deltaphi-Dependent Membrane Insertion of FtsQ
    • DOI 10.1074/jbc.M306527200
    • van der Laan M, Nouwen N, Driessen AJ (2004) SecYEG proteoliposomes catalyze the Deltaphi-dependent membrane insertion of FtsQ. J Biol Chem 279:1659-1664. (Pubitemid 38084432)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.3 , pp. 1659-1664
    • Van Der Laan, M.1    Nouwen, N.2    Driessen, A.J.M.3
  • 7
    • 0347192985 scopus 로고    scopus 로고
    • X-ray structure of a protein-conducting channel
    • Van den Berg B, et al. (2004) X-ray structure of a protein-conducting channel. Nature 427:36-44.
    • (2004) Nature , vol.427 , pp. 36-44
    • Van Den Berg, B.1
  • 8
    • 54049151196 scopus 로고    scopus 로고
    • Conformational transition of Sec machinery inferred from bacterial SecYE structures
    • Tsukazaki T, et al. (2008) Conformational transition of Sec machinery inferred from bacterial SecYE structures. Nature 455:988-991.
    • (2008) Nature , vol.455 , pp. 988-991
    • Tsukazaki, T.1
  • 9
    • 33947717366 scopus 로고    scopus 로고
    • Protein translocation is mediated by oligomers of the SecY complex with one SecY copy forming the channel
    • Osborne AR, Rapoport TA (2007) Protein translocation is mediated by oligomers of the SecY complex with one SecY copy forming the channel. Cell 129:97-110.
    • (2007) Cell , vol.129 , pp. 97-110
    • Osborne, A.R.1    Rapoport, T.A.2
  • 10
    • 54049111011 scopus 로고    scopus 로고
    • Structure of a complex of the ATPase SecA and the protein-translocation channel
    • Zimmer J, Nam Y, Rapoport TA (2008) Structure of a complex of the ATPase SecA and the protein-translocation channel. Nature 455:936-943.
    • (2008) Nature , vol.455 , pp. 936-943
    • Zimmer, J.1    Nam, Y.2    Rapoport, T.A.3
  • 11
    • 54049142467 scopus 로고    scopus 로고
    • A role for the two-helix finger of the SecA ATPase in protein translocation
    • Erlandson KJ, et al. (2008) A role for the two-helix finger of the SecA ATPase in protein translocation. Nature 455:984-987.
    • (2008) Nature , vol.455 , pp. 984-987
    • Erlandson, K.J.1
  • 13
    • 0036525752 scopus 로고    scopus 로고
    • Sec61β - A component of the archaeal protein secretory system
    • Kinch LN, Saier MH, Jr., Grishin NV (2002) Sec61β - a component of the archaeal protein secretory system. Trends Biochem Sci 27:170-171.
    • (2002) Trends Biochem Sci , vol.27 , pp. 170-171
    • Kinch, L.N.1    Saier Jr., M.H.2    Grishin, N.V.3
  • 14
    • 0032544614 scopus 로고    scopus 로고
    • Signal sequence recognition in posttranslational protein transport across the yeast ER membrane
    • DOI 10.1016/S0092-8674(00)81738-9
    • Plath K, Mothes W, Wilkinson BM, Stirling CJ, Rapoport TA (1998) Signal sequence recognition in posttranslational protein transport across the yeast ER membrane. Cell 94:795-807. (Pubitemid 28436011)
    • (1998) Cell , vol.94 , Issue.6 , pp. 795-807
    • Plath, K.1    Mothes, W.2    Wilkinson, B.M.3    Stirling, C.J.4    Rapoport, T.A.5
  • 15
    • 34248523155 scopus 로고    scopus 로고
    • The Plug Domain of the SecY Protein Stabilizes the Closed State of the Translocation Channel and Maintains a Membrane Seal
    • DOI 10.1016/j.molcel.2007.05.002, PII S1097276507002602
    • Li W, et al. (2007) The plug domain of the SecY protein stabilizes the closed state of the translocation channel and maintains a membrane seal. Mol Cell 26:511-521. (Pubitemid 46765185)
    • (2007) Molecular Cell , vol.26 , Issue.4 , pp. 511-521
    • Li, W.1    Schulman, S.2    Boyd, D.3    Erlandson, K.4    Beckwith, J.5    Rapoport, T.A.6
  • 17
    • 33748300566 scopus 로고    scopus 로고
    • The plug domain of yeast Sec61p is important for efficient protein translocation, but is not essential for cell viability
    • DOI 10.1091/mbc.E06-03-0200
    • Junne T, Schwede T, Goder V, Spiess M (2006) The plug domain of yeast Sec61p is important for efficient protein translocation, but is not essential for cell viability. Mol Biol Cell 17:4063-4068. (Pubitemid 44330888)
    • (2006) Molecular Biology of the Cell , vol.17 , Issue.9 , pp. 4063-4068
    • Junne, T.1    Schwede, T.2    Goder, V.3    Spiess, M.4
  • 18
    • 12144272096 scopus 로고    scopus 로고
    • Identification of cytoplasmic residues of Sec61p involved in ribosome binding and cotranslational translocation
    • DOI 10.1083/jcb.200408188
    • Cheng Z, Jiang Y, Mandon EC, Gilmore R (2005) Identification of cytoplasmic residues of Sec61p involved in ribosome binding and cotranslational translocation. J Cell Biol 168:67-77. (Pubitemid 40111058)
    • (2005) Journal of Cell Biology , vol.168 , Issue.1 , pp. 67-77
    • Cheng, Z.1    Jiang, Y.2    Mandon, E.C.3    Gilmore, R.4
  • 20
  • 22
    • 67650173024 scopus 로고    scopus 로고
    • The lateral gate of SecYEG opens during protein translocation
    • du Plessis DJ, Berrelkamp G, Nouwen N, Driessen AJ (2009) The lateral gate of SecYEG opens during protein translocation. J Biol Chem 284:15805-15814.
    • (2009) J Biol Chem , vol.284 , pp. 15805-15814
    • Du Plessis, D.J.1    Berrelkamp, G.2    Nouwen, N.3    Driessen, A.J.4
  • 23
    • 1542358892 scopus 로고    scopus 로고
    • Nascent membrane and secretory proteins differ in FRET-detected folding far inside the ribosome and in their exposure to ribosomal proteins
    • Woolhead CA, McCormick PJ, Johnson AE (2004) Nascent membrane and secretory proteins differ in FRET-detected folding far inside the ribosome and in their exposure to ribosomal proteins. Cell 116:725-736.
    • (2004) Cell , vol.116 , pp. 725-736
    • Woolhead, C.A.1    McCormick, P.J.2    Johnson, A.E.3
  • 24
    • 77949270274 scopus 로고    scopus 로고
    • α-helical nascent polypeptide chains visualized within distinct regions of the ribosomal exit tunnel
    • Bhushan S, et al. (2010) α-helical nascent polypeptide chains visualized within distinct regions of the ribosomal exit tunnel. Nat Struct Mol Biol 17:313-317.
    • (2010) Nat Struct Mol Biol , vol.17 , pp. 313-317
    • Bhushan, S.1
  • 26
    • 37249037182 scopus 로고    scopus 로고
    • Molecular code for transmembrane-helix recognition by the Sec61 translocon
    • Hessa T, et al. (2007) Molecular code for transmembrane-helix recognition by the Sec61 translocon. Nature 450:1026-1030.
    • (2007) Nature , vol.450 , pp. 1026-1030
    • Hessa, T.1
  • 27
    • 4944228608 scopus 로고    scopus 로고
    • Topogenesis of membrane proteins at the endoplasmic reticulum
    • Higy M, Junne T, Spiess M (2004) Topogenesis of membrane proteins at the endoplasmic reticulum. Biochemistry 43:12716-12722.
    • (2004) Biochemistry , vol.43 , pp. 12716-12722
    • Higy, M.1    Junne, T.2    Spiess, M.3
  • 28
    • 13544259578 scopus 로고    scopus 로고
    • Probing the environment of signal-anchor sequences during topogenesis in the endoplasmic reticulum
    • Higy M, Gander S, Spiess M (2005) Probing the environment of signal-anchor sequences during topogenesis in the endoplasmic reticulum. Biochemistry 44:2039-2047.
    • (2005) Biochemistry , vol.44 , pp. 2039-2047
    • Higy, M.1    Gander, S.2    Spiess, M.3
  • 29
    • 0029555914 scopus 로고
    • Protein insertion into the membrane of the endoplasmic reticulum: The architecture of the translocation site
    • Martoglio B, Dobberstein B (1995) Protein insertion into the membrane of the endoplasmic reticulum: The architecture of the translocation site. Cold Spring Harb Symp Quant Biol 60:41-45.
    • (1995) Cold Spring Harb Symp Quant Biol , vol.60 , pp. 41-45
    • Martoglio, B.1    Dobberstein, B.2
  • 30
    • 0029002962 scopus 로고
    • The protein-conducting channel in the membrane of the endoplasmic reticulum is open laterally toward the lipid bilayer
    • Martoglio B, Hofmann MW, Brunner J, Dobberstein B (1995) The protein-conducting channel in the membrane of the endoplasmic reticulum is open laterally toward the lipid bilayer. Cell 81:207-214.
    • (1995) Cell , vol.81 , pp. 207-214
    • Martoglio, B.1    Hofmann, M.W.2    Brunner, J.3    Dobberstein, B.4
  • 31
    • 33646271115 scopus 로고    scopus 로고
    • Molecular dynamics studies of the archaeal translocon
    • Gumbart J, Schulten K (2006) Molecular dynamics studies of the archaeal translocon. Biophys J 90:2356-2367.
    • (2006) Biophys J , vol.90 , pp. 2356-2367
    • Gumbart, J.1    Schulten, K.2
  • 32
    • 34848895197 scopus 로고    scopus 로고
    • Structural determinants of lateral gate opening in the protein translocon
    • Gumbart J, Schulten K (2007) Structural determinants of lateral gate opening in the protein translocon. Biochemistry 46:11147-11157.
    • (2007) Biochemistry , vol.46 , pp. 11147-11157
    • Gumbart, J.1    Schulten, K.2
  • 33
    • 59649110315 scopus 로고    scopus 로고
    • The roles of pore ring and plug in the SecY protein-conducting channel
    • Gumbart J, Schulten K (2008) The roles of pore ring and plug in the SecY protein-conducting channel. J Gen Physiol 132:709-719.
    • (2008) J Gen Physiol , vol.132 , pp. 709-719
    • Gumbart, J.1    Schulten, K.2
  • 34
    • 0042313962 scopus 로고    scopus 로고
    • Molecular mechanism of signal sequence orientation in the endoplasmic reticulum
    • Goder V, Spiess M (2003) Molecular mechanism of signal sequence orientation in the endoplasmic reticulum. EMBO J 22:3645-3653.
    • (2003) EMBO J , vol.22 , pp. 3645-3653
    • Goder, V.1    Spiess, M.2
  • 35
    • 1542313960 scopus 로고    scopus 로고
    • Sec61p contributes to signal sequence orientation according to the positive-inside rule
    • Goder V, Junne T, Spiess M (2004) Sec61p contributes to signal sequence orientation according to the positive-inside rule. Mol Biol Cell 15:1470-1478.
    • (2004) Mol Biol Cell , vol.15 , pp. 1470-1478
    • Goder, V.1    Junne, T.2    Spiess, M.3
  • 36
    • 36349034451 scopus 로고    scopus 로고
    • Mutations in the Sec61p channel affecting signal sequence recognition and membrane protein topology
    • Junne T, Schwede T, Goder V, Spiess M (2007) Mutations in the Sec61p channel affecting signal sequence recognition and membrane protein topology. J Biol Chem 282:33201-33209.
    • (2007) J Biol Chem , vol.282 , pp. 33201-33209
    • Junne, T.1    Schwede, T.2    Goder, V.3    Spiess, M.4
  • 37
    • 27144549973 scopus 로고    scopus 로고
    • Sequential triage of transmembrane segments by Sec61α during biogenesis of a native multispanning membrane protein
    • Sadlish H, Pitonzo D, Johnson AE, Skach WR (2005) Sequential triage of transmembrane segments by Sec61α during biogenesis of a native multispanning membrane protein. Nat Struct Mol Biol 12:870-878.
    • (2005) Nat Struct Mol Biol , vol.12 , pp. 870-878
    • Sadlish, H.1    Pitonzo, D.2    Johnson, A.E.3    Skach, W.R.4
  • 38
    • 51049088654 scopus 로고    scopus 로고
    • Control of translocation through the Sec61 translocon by nascent polypeptide structure within the ribosome
    • Daniel CJ, Conti B, Johnson AE, Skach WR (2008) Control of translocation through the Sec61 translocon by nascent polypeptide structure within the ribosome. J Biol Chem 283:20864-20873.
    • (2008) J Biol Chem , vol.283 , pp. 20864-20873
    • Daniel, C.J.1    Conti, B.2    Johnson, A.E.3    Skach, W.R.4
  • 39
    • 55849105200 scopus 로고    scopus 로고
    • Structures of SRP54 and SRP19, the two proteins that organize the ribonucleic core of the signal recognition particle from Pyrococcus furiosus
    • Egea PF, Napetschnig J, Walter P, Stroud RM (2008) Structures of SRP54 and SRP19, the two proteins that organize the ribonucleic core of the signal recognition particle from Pyrococcus furiosus. PLoS ONE 3:e3528.
    • (2008) PLoS ONE , vol.3
    • Egea, P.F.1    Napetschnig, J.2    Walter, P.3    Stroud, R.M.4
  • 40
    • 56149106957 scopus 로고    scopus 로고
    • Structures of the signal recognition particle receptor from the archaeon Pyrococcus furiosus: Implications for the targeting step at the membrane
    • Egea PF, et al. (2008) Structures of the signal recognition particle receptor from the archaeon Pyrococcus furiosus: Implications for the targeting step at the membrane. PLoS ONE 3:e3619.
    • (2008) PLoS ONE , vol.3
    • Egea, P.F.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.