X-ray structure of a protein-conducting channel (original) (raw)
References
Matlack, K. E. S., Mothes, W. & Rapoport, T. A. Protein translocation—tunnel vision. Cell92, 381–390 (1998) ArticleCAS Google Scholar
Simon, S. M. & Blobel, G. A protein-conducting channel in the endoplasmic reticulum. Cell65, 371–380 (1991) ArticleCAS Google Scholar
Crowley, K. S., Liao, S. R., Worrell, V. E., Reinhart, G. D. & Johnson, A. E. Secretory proteins move through the endoplasmic reticulum membrane via an aqueous, gated pore. Cell78, 461–471 (1994) ArticleCAS Google Scholar
Rapoport, T. A., Jungnickel, B. & Kutay, U. Protein transport across the eukaryotic endoplasmic reticulum and bacterial inner membranes. Annu. Rev. Biochem.65, 271–303 (1996) ArticleCAS Google Scholar
Mothes, W., Prehn, S. & Rapoport, T. A. Systematic probing of the environment of a translocating secretory protein during translocation through the ER membrane. EMBO J.13, 3937–3982 (1994) Article Google Scholar
Brundage, L., Hendrick, J. P., Schiebel, E., Driessen, A. J. M. & Wickner, W. The purified E. coli integral membrane protein SecY/E is sufficient for reconstitution of SecA-dependent precursor protein translocation. Cell62, 649–657 (1990) ArticleCAS Google Scholar
Gorlich, D. & Rapoport, T. A. Protein translocation into proteoliposomes reconstituted from purified components of the endoplasmic reticulum membrane. Cell75, 615–630 (1993) ArticleCAS Google Scholar
Deshaies, R. J., Sanders, S. L., Feldheim, D. A. & Schekman, R. Assembly of yeast Sec proteins involved in translocation into the endoplasmic reticulum into a membrane-bound multisubunit complex. Nature349, 806–808 (1991) ArticleADSCAS Google Scholar
Panzner, S., Dreier, L., Hartmann, E., Kostka, S. & Rapoport, T. A. Posttranslational protein transport in yeast reconstituted with a purified complex of Sec proteins and Kar2p. Cell81, 561–570 (1995) ArticleCAS Google Scholar
Matlack, K. E., Misselwitz, B., Plath, K. & Rapoport, T. A. BiP acts as a molecular ratchet during posttranslational transport of prepro-α-factor across the ER membrane. Cell97, 553–564 (1999) ArticleCAS Google Scholar
Economou, A. & Wickner, W. SecA promotes preprotein translocation by undergoing ATP-driven cycles of membrane insertion and deinsertion. Cell78, 835–843 (1994) ArticleCAS Google Scholar
Schiebel, E., Driessen, A. J. M., Hartl, F.-U. & Wickner, W. ΔµH+ and ATP function at different steps of the catalytic cycle of preprotein translocase. Cell64, 927–939 (1991) ArticleCAS Google Scholar
Irihimovitch, V. & Eichler, J. Post-translational secretion of fusion proteins in the halophilic archaea Haloferax volcanii.. J. Biol. Chem.278, 12881–12887 (2003) ArticleCAS Google Scholar
Hanein, D. et al. Oligomeric rings of the Sec61p complex induced by ligands required for protein translocation. Cell87, 721–732 (1996) ArticleCAS Google Scholar
Beckmann, R. et al. Alignment of conduits for the nascent polypeptide chain in the ribosome-Sec61 complex. Science19, 2123–2126 (1997) ArticleADS Google Scholar
Menetret, J. et al. The structure of ribosome-channel complexes engaged in protein translocation. Mol. Cell6, 1219–1232 (2000) ArticleCAS Google Scholar
Beckmann, R. et al. Architecture of the protein-conducting channel associated with the translating 80S ribosome. Cell107, 361–372 (2001) ArticleCAS Google Scholar
Morgan, D. G., Menetret, J. F., Neuhof, A., Rapoport, T. A. & Akey, C. W. Structure of the mammalian ribosome-channel complex at 17Å resolution. J. Mol. Biol.324, 871–886 (2002) ArticleCAS Google Scholar
Breyton, C., Haase, W., Rapoport, T. A., Kuhlbrandt, W. & Collinson, I. Three-dimensional structure of the bacterial protein-translocation complex SecYEG. Nature418, 662–665 (2002) ArticleADSCAS Google Scholar
Murata, K. et al. Structural determinants of water permeation through aquaporin-1. Nature407, 599–605 (2000) ArticleADSCAS Google Scholar
Dutzler, R., Campbell, E. B., Cadene, M., Chait, B. T. & MacKinnon, R. X-ray structure of a ClC chloride channel at 3.0 A reveals the molecular basis of anion selectivity. Nature415, 287–294 (2002) ArticleADSCAS Google Scholar
Flower, A. M., Osborne, R. S. & Silhavy, T. J. The allele-specific synthetic lethality of prlA-prlG double mutants predicts interactive domains of SecY and SecE. EMBO J.14, 884–893 (1995) ArticleCAS Google Scholar
Murphy, C. K. & Beckwith, J. Residues essential for the function of SecE, a membrane component of the Escherichia coli secretion apparatus, are located in a conserved cytoplasmic region. Proc. Natl Acad. Sci. USA91, 2557–2561 (1994) ArticleADSCAS Google Scholar
Satoh, Y., Mori, H. & Ito, K. Nearest neighbor analysis of the SecYEG complex. 2. Identification of a SecY-SecE cytosolic interface. Biochemistry42, 7442–7447 (2003) ArticleCAS Google Scholar
Nishiyama, K., Suzuki, T. & Tokuda, H. Inversion of the membrane topology of SecG coupled with SecA-dependent preprotein translocation. Cell85, 71–81 (1996) ArticleCAS Google Scholar
Harris, C. R. & Silhavy, T. J. Mapping an interface of SecY (PrlA) and SecE (PrlG) by using synthetic phenotypes and in vivo cross-linking. J. Bacteriol.181, 3438–3444 (1999) CASPubMedPubMed Central Google Scholar
Hamman, B. D., Hendershot, L. M. & Johnson, A. E. BiP maintains the permeability barrier of the ER membrane by sealing the lumenal end of the translocon pore before and early in translocation. Cell92, 747–758 (1998) ArticleCAS Google Scholar
Kurzchalia, T. V. et al. tRNA-mediated labelling of proteins with biotin. A nonradioactive method for the detection of cell-free translation products. Eur. J. Biochem.172, 663–668 (1988) ArticleCAS Google Scholar
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) CASPubMed Google Scholar
Mingarro, I., Nilsson, I., Whitley, P. & von Heijne, G. Different conformations of nascent polypeptides during translocation across the ER membrane. BMC Cell Biol.1, 3 (2000) ArticleCAS Google Scholar
Kowarik, M., Kung, S., Martoglio, B. & Helenius, A. Protein folding during cotranslational translocation in the endoplasmic reticulum. Mol. Cell10, 769–778 (2002) ArticleCAS Google Scholar
Hamman, B. D., Chen, J. C., Johnson, E. E. & Johnson, A. E. The aqueous pore through the translocon has a diameter of 40–60Å during cotranslational protein translocation at the ER membrane. Cell89, 535–544 (1997) ArticleCAS Google Scholar
Jungnickel, B. & Rapoport, T. A. A posttargeting signal sequence recognition event in the endoplasmic reticulum membrane. Cell82, 261–270 (1995) ArticleCAS Google Scholar
Plath, K., Mothes, W., Wilkinson, B. M., Stirling, C. J. & Rapoport, T. A. Signal sequence recognition in posttranslational protein transport across the yeast ER membrane. Cell94, 795–807 (1998) ArticleCAS Google Scholar
Heinrich, S. U., Mothes, W., Brunner, J. & Rapoport, T. A. The Sec61p complex mediates the integration of a membrane protein by allowing lipid partitioning of the transmembrane domain. Cell102, 233–244 (2000) ArticleCAS Google Scholar
Bieker, K. L., Phillips, G. J. & Silhavy, T. J. The sec and prl genes of Escherichia coli.. J. Bioenerg. Biomembr.22, 291–310 (1990) ArticleCAS Google Scholar
Derman, A. I., Puziss, J. W., Bassford, P. J. & Beckwith, J. A signal sequence is not required for protein export in prlA mutants of Escherichia coli. EMBO J.12, 879–888 (1993) ArticleCAS Google Scholar
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) ArticleCAS Google Scholar
Prinz, A., Behrens, C., Rapoport, T. A., Hartmann, E. & Kalies, K. U. Evolutionarily conserved binding of ribosomes to the translocation channel via the large ribosomal RNA. EMBO J.19, 1900–1906 (2000) ArticleCAS Google Scholar
Mori, H. & Ito, K. The Sec protein-translocation pathway. Trends Microbiol.9, 494–500 (2001) ArticleCAS Google Scholar
Kim, Y. J., Rajapandi, T. & Oliver, D. SecA protein is exposed to the periplasmic surface of the E.coli inner membrane in its active state. Cell78, 845–853 (1994) ArticleCAS Google Scholar
Heritage, D. & Wonderlin, W. F. Translocon pores in the endoplasmic reticulum are permeable to a neutral, polar molecule. J. Biol. Chem.276, 22655–22662 (2001) ArticleCAS Google Scholar
Manting, E. H., van Der Does, C., Remigy, H., Engel, A. & Driessen, A. J. SecYEG assembles into a tetramer to form the active protein translocation channel. EMBO J.19, 852–861 (2000) ArticleCAS Google Scholar
Mori, H. et al. Fluorescence resonance energy transfer analysis of protein translocase. SecYE from Thermus thermophilus HB8 forms a constitutive oligomer in membranes. J. Biol. Chem.278, 14257–14264 (2003) ArticleCAS Google Scholar
Duong, F. Binding, activation and dissociation of the dimeric SecA ATPase at the dimeric SecYEG translocase. EMBO J.22, 4375–4384 (2003) ArticleCAS Google Scholar
Kaufmann, A., Manting, E. H., Veenendaal, A. K., Driessen, A. J. & van der Does, C. Cysteine-directed cross-linking demonstrates that helix 3 of SecE is close to helix 2 of SecY and helix 3 of a neighboring SecE. Biochemistry38, 9115–9125 (1999) ArticleCAS Google Scholar
van der Sluis, E. O., Nouwen, N. & Driessen, A. J. SecY–SecY and SecY–SecG contacts revealed by site-specific crosslinking. FEBS Lett.527, 159–165 (2002) ArticleCAS Google Scholar
Yahr, T. L. & Wickner, W. T. Evaluating the oligomeric state of SecYEG in preprotein translocase. EMBO J.19, 4393–4401 (2000) ArticleCAS Google Scholar
Veenendaal, A. K., van der Does, C. & Driessen, A. J. Mapping the sites of interaction between SecY and SecE by cysteine scanning mutagenesis. J. Biol. Chem.276, 32559–32566 (2001) ArticleCAS Google Scholar
Plath, K., Wilkinson, B. M., Stirling, C. J. & Rapoport, T. A. Interactions between Sec-complex and prepro-α-factor during posttranslational protein transport into the ER. Mol. Biol. Cell (in the press)