메뉴 건너뛰기




Volumn 438, Issue 7066, 2005, Pages 318-324

Structure of the E. coli protein-conducting channel bound to a translating ribosome

Author keywords

[No Author keywords available]

Indexed keywords

ELECTRON MICROSCOPY; LIPIDS; PROTEINS; RNA;

EID: 27844444793     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature04133     Document Type: Article
Times cited : (220)

References (49)
  • 1
    • 0025854858 scopus 로고
    • A protein-conducting channel in the endoplasmic reticulum
    • Simon, S. M. & Blobel, G. A protein-conducting channel in the endoplasmic reticulum. Cell 65, 371-380 (1991).
    • (1991) Cell , vol.65 , pp. 371-380
    • Simon, S.M.1    Blobel, G.2
  • 2
    • 0025885002 scopus 로고
    • The enzymology of protein translocation across the Escherichia coli plasma membrane
    • Wickner, W., Driessen, A. J. M. & Hartl, F. U. The enzymology of protein translocation across the Escherichia coli plasma membrane. Annu. Rev. Biochem. 60, 101-124 (1991).
    • (1991) Annu. Rev. Biochem. , vol.60 , pp. 101-124
    • Wickner, W.1    Driessen, A.J.M.2    Hartl, F.U.3
  • 3
    • 0025087853 scopus 로고
    • The purified E. coli integral membrane protein SecY/E is sufficient for reconstitution of SecA-dependent precursor protein translocation
    • Brundage, L. et al. The purified E. coli integral membrane protein SecY/E is sufficient for reconstitution of SecA-dependent precursor protein translocation. Cell 62, 649-657 (1990).
    • (1990) Cell , vol.62 , pp. 649-657
    • Brundage, L.1
  • 4
    • 0027424601 scopus 로고
    • Protein translocation into proteoliposomes reconstituted from purified components of the endoplasmic reticulum membrane
    • Gorlich, D. & Rapoport, T. A. Protein translocation into proteoliposomes reconstituted from purified components of the endoplasmic reticulum membrane. Cell 75, 615-630 (1993).
    • (1993) Cell , vol.75 , pp. 615-630
    • Gorlich, D.1    Rapoport, T.A.2
  • 5
    • 0022129497 scopus 로고
    • Translocation of secretory proteins across the microsomal membrane occurs through an environment accessible to aqueous perturbants
    • Gilmore, R. & Blobel, G. Translocation of secretory proteins across the microsomal membrane occurs through an environment accessible to aqueous perturbants. Cell 42, 497-505 (1985).
    • (1985) Cell , vol.42 , pp. 497-505
    • Gilmore, R.1    Blobel, G.2
  • 6
    • 0040038098 scopus 로고
    • Large aqueous channels in membrane vesicles derived from the rough endoplasmic reticulum of canine pancreas or the plasma membrane of Escherichia coli
    • Simon, S. M., Blobel, G. & Zimmerberg, J. Large aqueous channels in membrane vesicles derived from the rough endoplasmic reticulum of canine pancreas or the plasma membrane of Escherichia coli. Proc. Natl Acad. Sci. USA 86, 6176-6180 (1989).
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 6176-6180
    • Simon, S.M.1    Blobel, G.2    Zimmerberg, J.3
  • 7
    • 0030825974 scopus 로고    scopus 로고
    • Molecular mechanism of membrane protein integration into the endoplasmic reticulum
    • Mothes, W. et al. Molecular mechanism of membrane protein integration into the endoplasmic reticulum. Cell 89, 523-533 (1997).
    • (1997) Cell , vol.89 , pp. 523-533
    • Mothes, W.1
  • 8
    • 13444262028 scopus 로고    scopus 로고
    • Recognition of transmembrane helices by the endoplasmic reticulum translocon
    • Hessa, T. et al. Recognition of transmembrane helices by the endoplasmic reticulum translocon. Nature 433, 377-381 (2005).
    • (2005) Nature , vol.433 , pp. 377-381
    • Hessa, T.1
  • 9
    • 0031473345 scopus 로고    scopus 로고
    • Alignment of conduits for the nascent polypeptide chain in the ribosome-Sec61 complex
    • Beckmann, R. et al. Alignment of conduits for the nascent polypeptide chain in the ribosome-Sec61 complex. Science 278, 2123-2126 (1997).
    • (1997) Science , vol.278 , pp. 2123-2126
    • Beckmann, R.1
  • 10
    • 0033638455 scopus 로고    scopus 로고
    • The structure of ribosome-channel complexes engaged in protein translocation
    • Menetret, J.-F. et al. The structure of ribosome-channel complexes engaged in protein translocation. Mol. Cell 6, 1219-1232 (2000).
    • (2000) Mol. Cell , vol.6 , pp. 1219-1232
    • Menetret, J.-F.1
  • 11
    • 0035798359 scopus 로고    scopus 로고
    • Architecture of the protein-conducting channel associated with the translating 80S ribosome
    • Beckmann, R. et al. Architecture of the protein-conducting channel associated with the translating 80S ribosome. Cell 107, 361-372 (2001).
    • (2001) Cell , vol.107 , pp. 361-372
    • Beckmann, R.1
  • 12
    • 0036927080 scopus 로고    scopus 로고
    • Structure of the mammalian ribosome-channel complex at 17 Å resolution
    • Morgan, D. G. et al. Structure of the mammalian ribosome-channel complex at 17 Å resolution. J. Mol. Biol. 324, 871-886 (2002).
    • (2002) J. Mol. Biol. , vol.324 , pp. 871-886
    • Morgan, D.G.1
  • 13
    • 0347192985 scopus 로고    scopus 로고
    • X-ray structure of a protein-conducting channel
    • van den Berg, B. et al. X-ray structure of a protein-conducting channel. Nature 427, 36-44 (2004).
    • (2004) Nature , vol.427 , pp. 36-44
    • Van Den Berg, B.1
  • 14
    • 4644356464 scopus 로고    scopus 로고
    • Membrane-protein integration and the role of the translocation channel
    • Rapoport, T. A., Goder, V., Heinrich, S. U. & Matlack, K. E. Membrane-protein integration and the role of the translocation channel. Trends Cell Biol. 14, 568-575 (2004).
    • (2004) Trends Cell Biol. , vol.14 , pp. 568-575
    • Rapoport, T.A.1    Goder, V.2    Heinrich, S.U.3    Matlack, K.E.4
  • 15
    • 0034678632 scopus 로고    scopus 로고
    • Evolutionary conserved binding of ribosomes to the translocation channel via the large ribosomal tRNA
    • Prinz, A. et al. Evolutionary conserved binding of ribosomes to the translocation channel via the large ribosomal tRNA. EMBO J. 19, 1900-1906 (2000).
    • (2000) EMBO J. , vol.19 , pp. 1900-1906
    • Prinz, A.1
  • 16
    • 0034631835 scopus 로고    scopus 로고
    • Role of the cytoplasmic segments of Sec61α in the ribosome-binding and translocation-promoting activities of the Sec61 complex
    • Raden, D., Song, W. & Gilmore, R. Role of the cytoplasmic segments of Sec61α in the ribosome-binding and translocation-promoting activities of the Sec61 complex. J. Cell Biol. 150, 53-64 (2000).
    • (2000) J. Cell Biol. , vol.150 , pp. 53-64
    • Raden, D.1    Song, W.2    Gilmore, R.3
  • 17
    • 12144272096 scopus 로고    scopus 로고
    • Identification of cytoplasmic residues of Sec61p involved in ribosome binding and cotranslational translocation
    • Cheng, Z., Jiang, Y., Mandon, E. C. & Gilmore, R. Identification of cytoplasmic residues of Sec61p involved in ribosome binding and cotranslational translocation. J. Cell Biol. 168, 67-77 (2005).
    • (2005) J. Cell Biol. , vol.168 , pp. 67-77
    • Cheng, Z.1    Jiang, Y.2    Mandon, E.C.3    Gilmore, R.4
  • 18
    • 0037040411 scopus 로고    scopus 로고
    • The ribosomal exit tunnel functions as a discriminating gate
    • Nakatogawa, H. & Ito, K. The ribosomal exit tunnel functions as a discriminating gate. Cell 108, 629-636 (2002).
    • (2002) Cell , vol.108 , pp. 629-636
    • Nakatogawa, H.1    Ito, K.2
  • 19
    • 0036500974 scopus 로고    scopus 로고
    • The SecYEG preprotein translocation channel is a conformationally dynamic and dimeric structure
    • Bessonneau, P., Besson, V., Collinson, I. & Duong, F. The SecYEG preprotein translocation channel is a conformationally dynamic and dimeric structure. EMBO J. 21, 995-1003 (2002).
    • (2002) EMBO J. , vol.21 , pp. 995-1003
    • Bessonneau, P.1    Besson, V.2    Collinson, I.3    Duong, F.4
  • 20
    • 0037063356 scopus 로고    scopus 로고
    • SecY-SecY and SecY-SecG contacts revealed by site-specific crosslinking
    • van der Sluis, E. O., Nouwen, N. & Driessen, A. J. M. SecY-SecY and SecY-SecG contacts revealed by site-specific crosslinking. FEBS Lett. 527, 159-165 (2002).
    • (2002) FEBS Lett. , vol.527 , pp. 159-165
    • Van Der Sluis, E.O.1    Nouwen, N.2    Driessen, A.J.M.3
  • 21
    • 4344716056 scopus 로고    scopus 로고
    • III NMFF: Flexible high-resolution annotation of low-resolution experimental data from cryo-EM maps using normal mode analysis
    • Tama, F., Miyashita, O. & Brooks, C. L. III NMFF: Flexible high-resolution annotation of low-resolution experimental data from cryo-EM maps using normal mode analysis. J. Struct. Biol. 147, 315-326 (2004).
    • (2004) J. Struct. Biol. , vol.147 , pp. 315-326
    • Tama, F.1    Miyashita, O.2    Brooks, C.L.3
  • 22
    • 0020771265 scopus 로고
    • Dynamics of a small globular protein in terms of low-frequency vibrational modes
    • Go, N., Noguti, T. & Nishikawa, T. Dynamics of a small globular protein in terms of low-frequency vibrational modes. Proc. Natl Acad. Sci. USA 80, 3696-3700 (1983).
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 3696-3700
    • Go, N.1    Noguti, T.2    Nishikawa, T.3
  • 23
    • 0033551435 scopus 로고    scopus 로고
    • Cysteine-directed cross-linking demonstrates that helix 3 of SecE is close to helix 2 of SecY and helix 3 of a neighbouring SecE
    • Kaufmann, A. et al. Cysteine-directed cross-linking demonstrates that helix 3 of SecE is close to helix 2 of SecY and helix 3 of a neighbouring SecE. Biochemistry 38, 9115-9125 (1999).
    • (1999) Biochemistry , vol.38 , pp. 9115-9125
    • Kaufmann, A.1
  • 24
    • 0035980042 scopus 로고    scopus 로고
    • Mapping the sites of interaction between SecY and SecE by cysteine scanning mutagenesis
    • Veenendaal, A., van der Does, C. & Driessen, A. Mapping the sites of interaction between SecY and SecE by cysteine scanning mutagenesis. J. Biol. Chem. 276, 32559-32566 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 32559-32566
    • Veenendaal, A.1    Van Der Does, C.2    Driessen, A.3
  • 25
    • 0025005885 scopus 로고
    • Translocation of ProOmpA possessing an intramolecular disulfide bridge into membrane vesicles of Escherichia coli. Effect of membrane energization
    • Tani, K., Tokuda, H. & Mizushima, S. Translocation of ProOmpA possessing an intramolecular disulfide bridge into membrane vesicles of Escherichia coli. Effect of membrane energization. J. Biol. Chem. 265, 17341-17347 (1990).
    • (1990) J. Biol. Chem. , vol.265 , pp. 17341-17347
    • Tani, K.1    Tokuda, H.2    Mizushima, S.3
  • 26
    • 0042671220 scopus 로고    scopus 로고
    • The Sec61p complex is a dynamic precursor activated channel
    • Wirth, A. et al. The Sec61p complex is a dynamic precursor activated channel. Mol. Cell 12, 261-268 (2003).
    • (2003) Mol. Cell , vol.12 , pp. 261-268
    • Wirth, A.1
  • 27
    • 0029002962 scopus 로고
    • The protein-conducting channel in the membrane of the endoplasmic reticulum is open laterally toward the lipid bilayer
    • Martoglio, B., Hofmann, M. W., Brunner, J. & Dobberstein, B. The protein-conducting channel in the membrane of the endoplasmic reticulum is open laterally toward the lipid bilayer. Cell 81, 207-214 (1995).
    • (1995) Cell , vol.81 , pp. 207-214
    • Martoglio, B.1    Hofmann, M.W.2    Brunner, J.3    Dobberstein, B.4
  • 28
    • 0035951840 scopus 로고    scopus 로고
    • In vitro binding of ribosomes to the β subunit of the Sec61p protein translocation complex
    • Levy, R., Wiedmann, M. & Kreibich, G. In vitro binding of ribosomes to the β subunit of the Sec61p protein translocation complex. J. Biol. Chem. 276, 2340-2346 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 2340-2346
    • Levy, R.1    Wiedmann, M.2    Kreibich, G.3
  • 29
    • 0027217073 scopus 로고
    • A novel membrane protein involved in protein translocation across the cytoplasmic membrane of Escherichia coli
    • Nishiyama, K.-i., Mizushima, S. & Tokuda, H. A novel membrane protein involved in protein translocation across the cytoplasmic membrane of Escherichia coli. EMBO J. 12, 3409-3415 (1993).
    • (1993) EMBO J. , vol.12 , pp. 3409-3415
    • Nishiyama, K.-I.1    Mizushima, S.2    Tokuda, H.3
  • 30
    • 0025732834 scopus 로고
    • One of three transmembrane stretches is sufficient for the functioning of the SecE protein, a membrane component of the E. coli secretion machinery
    • Schatz, P. J. et al. One of three transmembrane stretches is sufficient for the functioning of the SecE protein, a membrane component of the E. coli secretion machinery. EMBO J. 10, 1749-1757 (1991).
    • (1991) EMBO J. , vol.10 , pp. 1749-1757
    • Schatz, P.J.1
  • 31
    • 0031781639 scopus 로고    scopus 로고
    • The β subunit of the Sec61 complex facilitates cotranslational protein transport and interacts with the signal peptidase during translocation
    • Kalies, K. U., Rapoport, T. A. & Hartmann, E. The β subunit of the Sec61 complex facilitates cotranslational protein transport and interacts with the signal peptidase during translocation. J. Cell Biol. 141, 887-894 (1998).
    • (1998) J. Cell Biol. , vol.141 , pp. 887-894
    • Kalies, K.U.1    Rapoport, T.A.2    Hartmann, E.3
  • 32
    • 0032544614 scopus 로고    scopus 로고
    • Signal sequence recognition in posttranslational protein transport across the yeast ER membrane
    • Plath, K. et al. Signal sequence recognition in posttranslational protein transport across the yeast ER membrane. Cell 94, 795-807 (1998).
    • (1998) Cell , vol.94 , pp. 795-807
    • Plath, K.1
  • 33
    • 0031030059 scopus 로고    scopus 로고
    • Discrete cross-linking products identified during membrane protein biosynthesis
    • Laird, V. & High, S. Discrete cross-linking products identified during membrane protein biosynthesis. J. Biol. Chem. 272, 1983-1989 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 1983-1989
    • Laird, V.1    High, S.2
  • 34
    • 0034651753 scopus 로고    scopus 로고
    • YidC, the E. coli homologue of mitochondrial Oxa1p, is a component of the Sec translocase
    • Scotti, P. A. et al. YidC, the E. coli homologue of mitochondrial Oxa1p, is a component of the Sec translocase. EMBO J. 19, 542-549 (2000).
    • (2000) EMBO J. , vol.19 , pp. 542-549
    • Scotti, P.A.1
  • 35
    • 0027454264 scopus 로고
    • Site-specific photocross-linking reveals that Sec61p and TRAM contact different regions of a membrane-inserted signal sequence
    • High, S. et al. Site-specific photocross-linking reveals that Sec61p and TRAM contact different regions of a membrane-inserted signal sequence. J. Biol. Chem. 268, 26745-26751 (1993).
    • (1993) J. Biol. Chem. , vol.268 , pp. 26745-26751
    • High, S.1
  • 36
    • 0032079702 scopus 로고    scopus 로고
    • The Escherichia coli SRP and SecB targeting pathways converge at the translocon
    • Valent, Q. A. et al. The Escherichia coli SRP and SecB targeting pathways converge at the translocon. EMBO J. 17, 2504-2512 (1998).
    • (1998) EMBO J. , vol.17 , pp. 2504-2512
    • Valent, Q.A.1
  • 37
    • 0034387983 scopus 로고    scopus 로고
    • SRP-dependent cotranslational targeting and SecA-dependent translocation analyzed as individual steps in the export of a bacterial protein
    • Neumann-Haefelin, C., Schafer, U., Muller, M. & Koch, H. G. SRP-dependent cotranslational targeting and SecA-dependent translocation analyzed as individual steps in the export of a bacterial protein. EMBO J. 19, 6419-6426 (2000).
    • (2000) EMBO J. , vol.19 , pp. 6419-6426
    • Neumann-Haefelin, C.1    Schafer, U.2    Muller, M.3    Koch, H.G.4
  • 38
    • 0142071834 scopus 로고    scopus 로고
    • Two-stage binding of SecA to the bacterial translocon regulates ribosome-translocon interaction
    • Zito, C. R. & Oliver, D. Two-stage binding of SecA to the bacterial translocon regulates ribosome-translocon interaction. J. Biol. Chem. 278, 40640-40646 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 40640-40646
    • Zito, C.R.1    Oliver, D.2
  • 39
    • 0024278072 scopus 로고
    • Electron microscopy and computer image averaging of ice-embedded large ribosomal subunits from Escherichia coli
    • Wagenknecht, T., Grassucci, R. & Frank, J. Electron microscopy and computer image averaging of ice-embedded large ribosomal subunits from Escherichia coli. J. Mol. Biol. 199, 137-147 (1988).
    • (1988) J. Mol. Biol. , vol.199 , pp. 137-147
    • Wagenknecht, T.1    Grassucci, R.2    Frank, J.3
  • 40
    • 0029975088 scopus 로고    scopus 로고
    • SPIDER and WEB: Processing and visualization of images in 3D electron microscopy and related fields
    • Frank, J. et al. SPIDER and WEB: processing and visualization of images in 3D electron microscopy and related fields. J. Struct. Biol. 116, 190-199 (1996).
    • (1996) J. Struct. Biol. , vol.116 , pp. 190-199
    • Frank, J.1
  • 41
    • 0036646535 scopus 로고    scopus 로고
    • Cryo-EM reveals an active role for aminoacyl-tRNA in the accommodation process
    • Valle, M. et al. Cryo-EM reveals an active role for aminoacyl-tRNA in the accommodation process. EMBO J. 21, 3557-3567 (2002).
    • (2002) EMBO J. , vol.21 , pp. 3557-3567
    • Valle, M.1
  • 42
    • 0034598935 scopus 로고    scopus 로고
    • Solution structure of the E. coli 70S ribosome at 11.5 Å resolution
    • Gabashvili, I. S. et al. Solution structure of the E. coli 70S ribosome at 11.5 Å resolution. Cell 100, 537-549 (2000).
    • (2000) Cell , vol.100 , pp. 537-549
    • Gabashvili, I.S.1
  • 43
    • 0001832403 scopus 로고
    • Restrained real-space macromolecular atomic refinement using a new resolution-dependent electron density function
    • Chapman, M. S. Restrained real-space macromolecular atomic refinement using a new resolution-dependent electron density function. Acta Crystallogr. A 51, 69-80 (1995).
    • (1995) Acta Crystallogr. A , vol.51 , pp. 69-80
    • Chapman, M.S.1
  • 44
    • 84913050729 scopus 로고
    • An efficient general-purpose least-squares refinement program for macromolecular structures
    • Tronrud, D. E., Ten Eyck, L. F. & Matthews, B. W. An efficient general-purpose least-squares refinement program for macromolecular structures. Acta Crystallogr. A 43, 489-501 (1987).
    • (1987) Acta Crystallogr. A , vol.43 , pp. 489-501
    • Tronrud, D.E.1    Ten Eyck, L.F.2    Matthews, B.W.3
  • 45
    • 0038275890 scopus 로고    scopus 로고
    • Study of the structural dynamics of the E. coli 70S ribosome using real-space refinement
    • Gao, H. et al. Study of the structural dynamics of the E. coli 70S ribosome using real-space refinement. Cell 113, 789-801 (2003).
    • (2003) Cell , vol.113 , pp. 789-801
    • Gao, H.1
  • 46
    • 3242712966 scopus 로고    scopus 로고
    • Alterations at the peptidyl transferase centre of the ribosome induced by the synergistic action of the streptogramins dalfopristin and quinupristin
    • Harms, J. M. et al. Alterations at the peptidyl transferase centre of the ribosome induced by the synergistic action of the streptogramins dalfopristin and quinupristin. BMC Biol. 2, 4 (2004).
    • (2004) BMC Biol. , vol.2 , pp. 4
    • Harms, J.M.1
  • 47
    • 0000197372 scopus 로고    scopus 로고
    • Large amplitude elastic motions in proteins from a single-parameter, atomic analysis
    • Tirion, M. M. Large amplitude elastic motions in proteins from a single-parameter, atomic analysis. Phys. Rev. Lett. 77, 1905-1908 (1996).
    • (1996) Phys. Rev. Lett. , vol.77 , pp. 1905-1908
    • Tirion, M.M.1
  • 48
    • 0037043724 scopus 로고    scopus 로고
    • Three-dimensional structure of the bacterial protein-translocation complex SecYEG
    • Breyton, C. et al. Three-dimensional structure of the bacterial protein-translocation complex SecYEG. Nature 418, 662-665 (2002).
    • (2002) Nature , vol.418 , pp. 662-665
    • Breyton, C.1
  • 49
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography NMR system: A new software suite for macromolecular structure determination
    • Brunger, A. T. et al. Crystallography NMR system: a new software suite for macromolecular structure determination. Acta Crystallogr. D 54, 905-921 (1998).
    • (1998) Acta Crystallogr. D , vol.54 , pp. 905-921
    • Brunger, A.T.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.