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Volumn 129, Issue 1, 2007, Pages 97-110

Protein Translocation Is Mediated by Oligomers of the SecY Complex with One SecY Copy Forming the Channel

Author keywords

CELLBIO; PROTEINS

Indexed keywords

ADENOSINE TRIPHOSPHATASE; OLIGOMER; POLYPEPTIDE; PROTEIN SECA; SECY PROTEIN;

EID: 33947717366     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cell.2007.02.036     Document Type: Article
Times cited : (125)

References (32)
  • 1
    • 0037043724 scopus 로고    scopus 로고
    • Three-dimensional structure of the bacterial protein-translocation complex SecYEG
    • Breyton C., Haase W., Rapoport T.A., Kuhlbrandt W., and Collinson I. Three-dimensional structure of the bacterial protein-translocation complex SecYEG. Nature 418 (2002) 662-665
    • (2002) Nature , vol.418 , pp. 662-665
    • Breyton, C.1    Haase, W.2    Rapoport, T.A.3    Kuhlbrandt, W.4    Collinson, I.5
  • 2
    • 0025087853 scopus 로고
    • The purified E. coli integral membrane protein SecY/E Is sufficient for reconstitution of SecA-dependent precursor proteintranslocation
    • Brundage L., Hendrick J.P., Schiebel E., Driessen A.J.M., and Wickner W. The purified E. coli integral membrane protein SecY/E Is sufficient for reconstitution of SecA-dependent precursor proteintranslocation. Cell 62 (1990) 649-657
    • (1990) Cell , vol.62 , pp. 649-657
    • Brundage, L.1    Hendrick, J.P.2    Schiebel, E.3    Driessen, A.J.M.4    Wickner, W.5
  • 3
    • 18544380083 scopus 로고    scopus 로고
    • Disulfide bridge formation between SecY and a translocating polypeptide localizes the translocation pore to the center of SecY
    • Cannon K.S., Or E., Clemons Jr. W.M., Shibata Y., and Rapoport T.A. Disulfide bridge formation between SecY and a translocating polypeptide localizes the translocation pore to the center of SecY. J. Cell Biol. 169 (2005) 219-225
    • (2005) J. Cell Biol. , vol.169 , pp. 219-225
    • Cannon, K.S.1    Or, E.2    Clemons Jr., W.M.3    Shibata, Y.4    Rapoport, T.A.5
  • 4
    • 0034637517 scopus 로고    scopus 로고
    • Distinct membrane binding properties of N- and C-terminal domains of Escherichia coli SecA ATPase
    • Dapic V., and Oliver D. Distinct membrane binding properties of N- and C-terminal domains of Escherichia coli SecA ATPase. J. Biol. Chem. 275 (2000) 25000-25007
    • (2000) J. Biol. Chem. , vol.275 , pp. 25000-25007
    • Dapic, V.1    Oliver, D.2
  • 5
    • 0041736710 scopus 로고    scopus 로고
    • Binding, activation and dissociation of the dimeric SecA ATPase at the dimeric SecYEG translocase
    • Duong F. Binding, activation and dissociation of the dimeric SecA ATPase at the dimeric SecYEG translocase. EMBO J. 22 (2003) 4375-4384
    • (2003) EMBO J. , vol.22 , pp. 4375-4384
    • Duong, F.1
  • 6
    • 0028064967 scopus 로고
    • SecA promotes preprotein translocation by undergoing ATP-driven cycles of membrane insertion and deinsertion
    • Economou A., and Wickner W. SecA promotes preprotein translocation by undergoing ATP-driven cycles of membrane insertion and deinsertion. Cell 78 (1994) 835-843
    • (1994) Cell , vol.78 , pp. 835-843
    • Economou, A.1    Wickner, W.2
  • 7
    • 2342633273 scopus 로고    scopus 로고
    • Break on through to the other side-the Sec translocon
    • Eichler J., and Duong F. Break on through to the other side-the Sec translocon. Trends Biochem. Sci. 29 (2004) 221-223
    • (2004) Trends Biochem. Sci. , vol.29 , pp. 221-223
    • Eichler, J.1    Duong, F.2
  • 8
    • 33646271115 scopus 로고    scopus 로고
    • Molecular dynamics studies of the archaeal translocon
    • Gumbart J., and Schulten K. Molecular dynamics studies of the archaeal translocon. Biophys. J. 90 (2006) 2356-2367
    • (2006) Biophys. J. , vol.90 , pp. 2356-2367
    • Gumbart, J.1    Schulten, K.2
  • 9
    • 0030611388 scopus 로고    scopus 로고
    • The aqueous pore through the translocon has a diameter of 40-60 Å during cotranslational protein translocation at the ER membrane
    • Hamman B.D., Chen J.C., Johnson E.E., and Johnson A.E. The aqueous pore through the translocon has a diameter of 40-60 Å during cotranslational protein translocation at the ER membrane. Cell 89 (1997) 535-544
    • (1997) Cell , vol.89 , pp. 535-544
    • Hamman, B.D.1    Chen, J.C.2    Johnson, E.E.3    Johnson, A.E.4
  • 10
    • 33746923016 scopus 로고    scopus 로고
    • Active and passive displacement of transmembrane domains both occur during opsin biogenesis at the Sec61 translocon
    • Ismail N., Crawshaw S.G., and High S. Active and passive displacement of transmembrane domains both occur during opsin biogenesis at the Sec61 translocon. J. Cell Sci. 119 (2006) 2826-2836
    • (2006) J. Cell Sci. , vol.119 , pp. 2826-2836
    • Ismail, N.1    Crawshaw, S.G.2    High, S.3
  • 11
    • 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 neighboring SecE
    • Kaufmann A., Manting E.H., Veenendaal A.K., Driessen A.J., and 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. Biochemistry 38 (1999) 9115-9125
    • (1999) Biochemistry , vol.38 , pp. 9115-9125
    • Kaufmann, A.1    Manting, E.H.2    Veenendaal, A.K.3    Driessen, A.J.4    van der Does, C.5
  • 12
    • 0036810271 scopus 로고    scopus 로고
    • Protein folding during cotranslational translocation in the endoplasmic reticulum
    • Kowarik M., Kung S., Martoglio B., and Helenius A. Protein folding during cotranslational translocation in the endoplasmic reticulum. Mol. Cell 10 (2002) 769-778
    • (2002) Mol. Cell , vol.10 , pp. 769-778
    • Kowarik, M.1    Kung, S.2    Martoglio, B.3    Helenius, A.4
  • 13
    • 33750580851 scopus 로고    scopus 로고
    • Co- and post-translational translocation through the protein-conducting channel: analogous mechanisms at work?
    • Mitra K., Frank J., and Driessen A. Co- and post-translational translocation through the protein-conducting channel: analogous mechanisms at work?. Nat. Struct. Mol. Biol. 13 (2006) 957-964
    • (2006) Nat. Struct. Mol. Biol. , vol.13 , pp. 957-964
    • Mitra, K.1    Frank, J.2    Driessen, A.3
  • 15
    • 0035942263 scopus 로고    scopus 로고
    • An essential amino acid residue in the protein translocation channel revealed by targeted random mutagenesis of SecY
    • Mori H., and Ito K. An essential amino acid residue in the protein translocation channel revealed by targeted random mutagenesis of SecY. Proc. Natl. Acad. Sci. USA 98 (2001) 5128-5133
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 5128-5133
    • Mori, H.1    Ito, K.2
  • 16
    • 33750844195 scopus 로고    scopus 로고
    • Different modes of SecY-SecA interactions revealed by site-directed in vivo photo-cross-linking
    • Mori H., and Ito K. Different modes of SecY-SecA interactions revealed by site-directed in vivo photo-cross-linking. Proc. Natl. Acad. Sci. USA 103 (2006) 16159-16164
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 16159-16164
    • Mori, H.1    Ito, K.2
  • 17
    • 0037687309 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer analysis of protein translocase. SecYE from Thermus thermophilus HB8 forms a constitutive oligomer in membranes
    • Mori H., Tsukazaki T., Masui R., Kuramitsu S., Yokoyama S., Johnson A.E., Kimura Y., Akiyama Y., and Ito K. Fluorescence resonance energy transfer analysis of protein translocase. SecYE from Thermus thermophilus HB8 forms a constitutive oligomer in membranes. J. Biol. Chem. 278 (2003) 14257-14264
    • (2003) J. Biol. Chem. , vol.278 , pp. 14257-14264
    • Mori, H.1    Tsukazaki, T.2    Masui, R.3    Kuramitsu, S.4    Yokoyama, S.5    Johnson, A.E.6    Kimura, Y.7    Akiyama, Y.8    Ito, K.9
  • 18
    • 15744404686 scopus 로고    scopus 로고
    • The bacterial ATPase SecA functions as a monomer In protein translocation
    • Or E., Boyd D., Gon S., Beckwith J., and Rapoport T. The bacterial ATPase SecA functions as a monomer In protein translocation. J. Biol. Chem. 280 (2004) 9097-9105
    • (2004) J. Biol. Chem. , vol.280 , pp. 9097-9105
    • Or, E.1    Boyd, D.2    Gon, S.3    Beckwith, J.4    Rapoport, T.5
  • 21
    • 0032544614 scopus 로고    scopus 로고
    • Signal sequence recognition in posttranslational protein transport across the yeast ER membrane
    • Plath K., Mothes W., Wilkinson B.M., Stirling C.J., and Rapoport T.A. Signal sequence recognition in posttranslational protein transport across the yeast ER membrane. Cell 94 (1998) 795-807
    • (1998) Cell , vol.94 , pp. 795-807
    • Plath, K.1    Mothes, W.2    Wilkinson, B.M.3    Stirling, C.J.4    Rapoport, T.A.5
  • 22
    • 0346099350 scopus 로고    scopus 로고
    • Interactions between Sec complex and prepro-alpha-factor during posttranslational protein transport into the endoplasmic reticulum
    • Plath K., Wilkinson B.M., Stirling C.J., and Rapoport T.A. Interactions between Sec complex and prepro-alpha-factor during posttranslational protein transport into the endoplasmic reticulum. Mol. Biol. Cell 15 (2004) 1-10
    • (2004) Mol. Biol. Cell , vol.15 , pp. 1-10
    • Plath, K.1    Wilkinson, B.M.2    Stirling, C.J.3    Rapoport, T.A.4
  • 23
    • 27144549973 scopus 로고    scopus 로고
    • Sequential triage of transmembrane segments by Sec61alpha during biogenesis of a native multispanning membrane protein
    • Sadlish H., Pitonzo D., Johnson A.E., and Skach W.R. Sequential triage of transmembrane segments by Sec61alpha during biogenesis of a native multispanning membrane protein. Nat. Struct. Mol. Biol. 12 (2005) 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
  • 24
    • 33748297447 scopus 로고    scopus 로고
    • Ribosome binding to and dissociation from translocation sites of the endoplasmic reticulum membrane
    • Schaletzky J., and Rapoport T.A. Ribosome binding to and dissociation from translocation sites of the endoplasmic reticulum membrane. Mol. Biol. Cell 17 (2006) 3860-3869
    • (2006) Mol. Biol. Cell , vol.17 , pp. 3860-3869
    • Schaletzky, J.1    Rapoport, T.A.2
  • 27
    • 27144525002 scopus 로고    scopus 로고
    • Investigating the SecY plug movement at the SecYEG translocation channel
    • Tam P.C., Maillard A.P., Chan K.K., and Duong F. Investigating the SecY plug movement at the SecYEG translocation channel. EMBO J. 24 (2005) 3380-3388
    • (2005) EMBO J. , vol.24 , pp. 3380-3388
    • Tam, P.C.1    Maillard, A.P.2    Chan, K.K.3    Duong, F.4
  • 28
    • 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., and Mizushima S. Translocation of proOmpA possessing an intramolecular disulfide bridge into membrane vesicles of Escherichia Coli. Effect of membrane energization. J. Biol. Chem. 265 (1990) 17341-17347
    • (1990) J. Biol. Chem. , vol.265 , pp. 17341-17347
    • Tani, K.1    Tokuda, H.2    Mizushima, S.3
  • 29
    • 18844384961 scopus 로고    scopus 로고
    • Protein secretion in the absence of ATP: the autotransporter, two-partner secretion and chaperone/usher pathways of gram-negative bacteria (review)
    • Thanassi D.G., Stathopoulos C., Karkal A., and Li H. Protein secretion in the absence of ATP: the autotransporter, two-partner secretion and chaperone/usher pathways of gram-negative bacteria (review). Mol. Membr. Biol. 22 (2005) 63-72
    • (2005) Mol. Membr. Biol. , vol.22 , pp. 63-72
    • Thanassi, D.G.1    Stathopoulos, C.2    Karkal, A.3    Li, H.4
  • 31
    • 33750846046 scopus 로고    scopus 로고
    • Crystal Structure of the Translocation ATPase SecA from Thermus thermophilus Reveals a Parallel, Head-to-Head Dimer
    • Vassylyev D.G., Mori H., Vassylyeva M.N., Tsukazaki T., Kimura Y., Tahirov T.H., and Ito K. Crystal Structure of the Translocation ATPase SecA from Thermus thermophilus Reveals a Parallel, Head-to-Head Dimer. J. Mol. Biol. 364 (2006) 248-258
    • (2006) J. Mol. Biol. , vol.364 , pp. 248-258
    • Vassylyev, D.G.1    Mori, H.2    Vassylyeva, M.N.3    Tsukazaki, T.4    Kimura, Y.5    Tahirov, T.H.6    Ito, K.7
  • 32
    • 33745628037 scopus 로고    scopus 로고
    • The geometry of the ribosomal polypeptide exit tunnel
    • Voss N.R., Gerstein M., Steitz T.A., and Moore P.B. The geometry of the ribosomal polypeptide exit tunnel. J. Mol. Biol. 360 (2006) 893-906
    • (2006) J. Mol. Biol. , vol.360 , pp. 893-906
    • Voss, N.R.1    Gerstein, M.2    Steitz, T.A.3    Moore, P.B.4


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