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Volumn 198, Issue 5, 2012, Pages 881-893

Bacterial protein translocation requires only one copy of the SecY complex in vivo

Author keywords

[No Author keywords available]

Indexed keywords

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

EID: 84866388574     PISSN: 00219525     EISSN: 15408140     Source Type: Journal    
DOI: 10.1083/jcb.201205140     Document Type: Article
Times cited : (43)

References (39)
  • 2
    • 0036500974 scopus 로고    scopus 로고
    • The SecYEG preprotein translocation channel is a conformationally dynamic and dimeric structure
    • Bessonneau, P., V. Besson, I. Collinson, and F. Duong. 2002. The SecYEG preprotein translocation channel is a conformationally dynamic and dimeric structure. EMBO J. 21: 995-1003. http://dx.doi.org/10.1093/ emboj/21.5.995
    • (2002) EMBO J , vol.21 , pp. 995-1003
    • Bessonneau, P.1    Besson, V.2    Collinson, I.3    Duong, F.4
  • 3
    • 0037043724 scopus 로고    scopus 로고
    • Three-dimensional structure of the bacterial protein-translocation complex SecYEG
    • Breyton, C., W. Haase, T.A. Rapoport, W. Kühlbrandt, and I. Collinson. 2002. Three-dimensional structure of the bacterial protein-translocation complex SecYEG. Nature. 418: 662-665. http://dx.doi.org/10.1038/nature00827
    • (2002) Nature , vol.418 , pp. 662-665
    • Breyton, C.1    Haase, W.2    Rapoport, T.A.3    Kühlbrandt, W.4    Collinson, I.5
  • 4
    • 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., E. Or, W.M. Clemons Jr., Y. Shibata, and T.A. Rapoport. 2005. Disulfide bridge formation between SecY and a translocating polypeptide localizes the translocation pore to the center of SecY. J. Cell Biol. 169: 219-225. http://dx.doi.org/10.1083/jcb.200412019
    • (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
  • 5
    • 84858238365 scopus 로고    scopus 로고
    • Two copies of the SecY channel and acidic lipids are necessary to activate the SecA translocation ATPase
    • Dalal, K., C.S. Chan, S.G. Sligar, and F. Duong. 2012. Two copies of the SecY channel and acidic lipids are necessary to activate the SecA translocation ATPase. Proc. Natl. Acad. Sci. USA. 109:4104-4109.
    • (2012) Proc. Natl. Acad. Sci. USA. , vol.109 , pp. 4104-4109
    • Dalal, K.1    Chan, C.S.2    Sligar, S.G.3    Duong, F.4
  • 6
    • 79953302604 scopus 로고    scopus 로고
    • Mapping of the SecA.SecY and SecA.SecG interfaces by site-directed in vivo photocross-linking
    • Das, S., and D.B. Oliver. 2011. Mapping of the SecA.SecY and SecA.SecG interfaces by site-directed in vivo photocross-linking. J. Biol. Chem. 286: 12371-12380. http://dx.doi.org/10.1074/jbc.M110.182931
    • (2011) J. Biol. Chem , vol.286 , pp. 12371-12380
    • Das, S.1    Oliver, D.B.2
  • 7
    • 0034612342 scopus 로고    scopus 로고
    • One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products
    • Datsenko, K.A., and B.L. Wanner. 2000. One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products. Proc. Natl. Acad. Sci. USA. 97: 6640-6645. http://dx.doi.org/10.1073/pnas.120163297
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 6640-6645
    • Datsenko, K.A.1    Wanner, B.L.2
  • 9
    • 84857132094 scopus 로고    scopus 로고
    • Ca2+ signaling amplification by oligomerization of L-type Cav1.2 channels
    • Dixon, R.E., C. Yuan, E.P. Cheng, M.F. Navedo, and L.F. Santana. 2012. Ca2+ signaling amplification by oligomerization of L-type Cav1.2 channels. Proc. Natl. Acad. Sci. USA. 109: 1749-1754. http://dx.doi.org/ 10.1073/pnas.1116731109
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 1749-1754
    • Dixon, R.E.1    Yuan, C.2    Cheng, E.P.3    Navedo, M.F.4    Santana, L.F.5
  • 10
    • 50649104037 scopus 로고    scopus 로고
    • Protein translocation across the bacterial cytoplasmic membrane
    • Driessen, A.J., and N. Nouwen. 2008. Protein translocation across the bacterial cytoplasmic membrane. Annu. Rev. Biochem. 77: 643-667. http://dx.doi .org/10.1146/annurev.biochem.77.061606.160747
    • (2008) Annu. Rev. Biochem , vol.77 , pp. 643-667
    • Driessen, A.J.1    Nouwen, N.2
  • 11
    • 0037327607 scopus 로고    scopus 로고
    • Involvement of helices at the dimer interface in ClC-1 common gating
    • Duffield, M., G. Rychkov, A. Bretag, and M. Roberts. 2003. Involvement of helices at the dimer interface in ClC-1 common gating. J. Gen. Physiol. 121: 149-161. http://dx.doi.org/10.1085/jgp.20028741
    • (2003) J. Gen. Physiol , vol.121 , pp. 149-161
    • Duffield, M.1    Rychkov, G.2    Bretag, A.3    Roberts, M.4
  • 12
    • 78049253482 scopus 로고    scopus 로고
    • Lateral opening of a translocon upon entry of protein suggests the mechanism of insertion into membranes
    • Egea, P.F., and R.M. Stroud. 2010. Lateral opening of a translocon upon entry of protein suggests the mechanism of insertion into membranes. Proc. Natl. Acad. Sci. USA. 107: 17182-17187. http://dx.doi.org/10.1073/ pnas.1012556107
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 17182-17187
    • Egea, P.F.1    Stroud, R.M.2
  • 15
    • 70350738240 scopus 로고    scopus 로고
    • Regulation of the protein-conducting channel by a bound ribosome
    • Gumbart, J., L.G. Trabuco, E. Schreiner, E. Villa, and K. Schulten. 2009. Regulation of the protein-conducting channel by a bound ribosome. Structure. 17: 1453-1464. http://dx.doi.org/10.1016/j.str.2009.09.010
    • (2009) Structure , vol.17 , pp. 1453-1464
    • Gumbart, J.1    Trabuco, L.G.2    Schreiner, E.3    Villa, E.4    Schulten, K.5
  • 16
    • 0030611388 scopus 로고    scopus 로고
    • The aqueous pore through the translocon has a diameter of 40-60 A during cotranslational protein translocation at the ER membrane
    • Hamman, B.D., J.C. Chen, E.E. Johnson, and A.E. Johnson. 1997. The aqueous pore through the translocon has a diameter of 40-60 A during cotranslational protein translocation at the ER membrane. Cell. 89: 535-544. http://dx.doi.org/10.1016/S0092-8674(00)80235-4
    • (1997) Cell , vol.89 , pp. 535-544
    • Hamman, B.D.1    Chen, J.C.2    Johnson, E.E.3    Johnson, A.E.4
  • 17
    • 0032549767 scopus 로고    scopus 로고
    • BiP maintains the permeability barrier of the ER membrane by sealing the lumenal end of the translocon pore before and early in translocation
    • Hamman, B.D., L.M. Hendershot, and A.E. Johnson. 1998. BiP maintains the permeability barrier of the ER membrane by sealing the lumenal end of the translocon pore before and early in translocation. Cell. 92: 747-758. http://dx.doi.org/10.1016/S0092-8674(00)81403-8
    • (1998) Cell , vol.92 , pp. 747-758
    • Hamman, B.D.1    Hendershot, L.M.2    Johnson, A.E.3
  • 18
    • 77249150932 scopus 로고    scopus 로고
    • Formation and dissociation of M1 muscarinic receptor dimers seen by total internal reflection fluorescence imaging of single molecules
    • Hern, J.A., A.H. Baig, G.I. Mashanov, B. Birdsall, J.E. Corrie, S. Lazareno, J.E. Molloy, and N.J. Birdsall. 2010. Formation and dissociation of M1 muscarinic receptor dimers seen by total internal reflection fluorescence imaging of single molecules. Proc. Natl. Acad. Sci. USA. 107: 2693-2698. http://dx.doi.org/10.1073/pnas.0907915107
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 2693-2698
    • Hern, J.A.1    Baig, A.H.2    Mashanov, G.I.3    Birdsall, B.4    Corrie, J.E.5    Lazareno, S.6    Molloy, J.E.7    Birdsall, N.J.8
  • 20
    • 79551711208 scopus 로고    scopus 로고
    • Full characterization of GPCR monomer-dimer dynamic equilibrium by single molecule imaging
    • Kasai, R.S., K.G. Suzuki, E.R. Prossnitz, I. Koyama-Honda, C. Nakada, T.K. Fujiwara, and A. Kusumi. 2011. Full characterization of GPCR monomer-dimer dynamic equilibrium by single molecule imaging. J. Cell Biol. 192: 463-480. http://dx.doi.org/10.1083/jcb.201009128
    • (2011) J. Cell Biol , vol.192 , pp. 463-480
    • Kasai, R.S.1    Suzuki, K.G.2    Prossnitz, E.R.3    Koyama-Honda, I.4    Nakada, C.5    Fujiwara, T.K.6    Kusumi, A.7
  • 21
    • 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., E.H. Manting, A.K. Veenendaal, A.J. Driessen, and C. van der Does. 1999. 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: 9115-9125. http://dx.doi.org/10.1021/bi990539d
    • (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
  • 22
    • 80455155003 scopus 로고    scopus 로고
    • A single copy of SecYEG is sufficient for preprotein translocation
    • Kedrov, A., I. Kusters, V.V. Krasnikov, and A.J. Driessen. 2011. A single copy of SecYEG is sufficient for preprotein translocation. EMBO J. 30: 4387-4397. http://dx.doi.org/10.1038/emboj.2011.314
    • (2011) EMBO J , vol.30 , pp. 4387-4397
    • Kedrov, A.1    Kusters, I.2    Krasnikov, V.V.3    Driessen, A.J.4
  • 23
    • 80053971494 scopus 로고    scopus 로고
    • Transmembrane segments of nascent polytopic membrane proteins control cytosol/ER targeting during membrane integration
    • Lin, P.J., C.G. Jongsma, S. Liao, and A.E. Johnson. 2011. Transmembrane segments of nascent polytopic membrane proteins control cytosol/ER targeting during membrane integration. J. Cell Biol. 195: 41-54. http:// dx.doi.org/10.1083/jcb.201103117
    • (2011) J. Cell Biol , vol.195 , pp. 41-54
    • Lin, P.J.1    Jongsma, C.G.2    Liao, S.3    Johnson, A.E.4
  • 25
    • 46049116259 scopus 로고    scopus 로고
    • Single copies of Sec61 and TRAP associate with a nontranslating mammalian ribosome
    • Ménétret, J.F., R.S. Hegde, M. Aguiar, S.P. Gygi, E. Park, T.A. Rapoport, and C.W. Akey. 2008. Single copies of Sec61 and TRAP associate with a nontranslating mammalian ribosome. Structure. 16: 1126-1137. http:// dx.doi.org/10.1016/j.str.2008.05.003
    • (2008) Structure , vol.16 , pp. 1126-1137
    • Ménétret, J.F.1    Hegde, R.S.2    Aguiar, M.3    Gygi, S.P.4    Park, E.5    Rapoport, T.A.6    Akey, C.W.7
  • 26
    • 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., T. Tsukazaki, R. Masui, S. Kuramitsu, S. Yokoyama, A.E. Johnson, Y. Kimura, Y. Akiyama, and K. Ito. 2003. 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. http://dx.doi.org/10.1074/jbc.M300230200
    • (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
  • 27
    • 0035105116 scopus 로고    scopus 로고
    • Secretion monitor, SecM, undergoes self- translation arrest in the cytosol
    • Nakatogawa, H., and K. Ito. 2001. Secretion monitor, SecM, undergoes self- translation arrest in the cytosol. Mol. Cell. 7: 185-192. http://dx.doi .org/10.1016/S1097-2765(01)00166-6
    • (2001) Mol. Cell , vol.7 , pp. 185-192
    • Nakatogawa, H.1    Ito, K.2
  • 28
    • 33947717366 scopus 로고    scopus 로고
    • Protein translocation is mediated by oligomers of the SecY complex with one SecY copy forming the channel
    • Osborne, A.R., and T.A. Rapoport. 2007. Protein translocation is mediated by oligomers of the SecY complex with one SecY copy forming the channel. Cell. 129: 97-110. http://dx.doi.org/10.1016/j.cell.2007.02.036
    • (2007) Cell , vol.129 , pp. 97-110
    • Osborne, A.R.1    Rapoport, T.A.2
  • 29
    • 79955901001 scopus 로고    scopus 로고
    • Preserving the membrane barrier for small molecules during bacterial protein translocation
    • Park, E., and T.A. Rapoport. 2011. Preserving the membrane barrier for small molecules during bacterial protein translocation. Nature. 473: 239-242. http://dx.doi.org/10.1038/nature10014
    • (2011) Nature , vol.473 , pp. 239-242
    • Park, E.1    Rapoport, T.A.2
  • 30
    • 84861361690 scopus 로고    scopus 로고
    • Mechanisms of Sec61/SecY-mediated protein translocation across membranes
    • Park, E., and T.A. Rapoport. 2012. Mechanisms of Sec61/SecY-mediated protein translocation across membranes. Annu Rev Biophys. 41: 21-40. http://dx.doi.org/10.1146/annurev-biophys-050511-102312
    • (2012) Annu Rev Biophys , vol.41 , pp. 21-40
    • Park, E.1    Rapoport, T.A.2
  • 31
    • 30544433196 scopus 로고    scopus 로고
    • Engineering and characterization of a superfolder green fluorescent protein
    • Pédelacq, J.D., S. Cabantous, T. Tran, T.C. Terwilliger, and G.S. Waldo. 2006. Engineering and characterization of a superfolder green fluorescent protein. Nat. Biotechnol. 24: 79-88. http://dx.doi.org/10.1038/nbt1172
    • (2006) Nat. Biotechnol , vol.24 , pp. 79-88
    • Pédelacq, J.D.1    Cabantous, S.2    Tran, T.3    Terwilliger, T.C.4    Waldo, G.S.5
  • 32
    • 33748297447 scopus 로고    scopus 로고
    • Ribosome binding to and dissociation from translocation sites of the endoplasmic reticulum membrane
    • Schaletzky, J., and T.A. Rapoport. 2006. Ribosome binding to and dissociation from translocation sites of the endoplasmic reticulum membrane. Mol. Biol. Cell. 17: 3860-3869. http://dx.doi.org/10.1091/mbc.E06-05-0439
    • (2006) Mol. Biol. Cell , vol.17 , pp. 3860-3869
    • Schaletzky, J.1    Rapoport, T.A.2
  • 34
    • 0141727632 scopus 로고    scopus 로고
    • The DsbA signal sequence directs efficient, cotranslational export of passenger proteins to the Escherichia coli periplasm via the signal recognition particle pathway
    • Schierle, C.F., M. Berkmen, D. Huber, C. Kumamoto, D. Boyd, and J. Beckwith. 2003. The DsbA signal sequence directs efficient, cotranslational export of passenger proteins to the Escherichia coli periplasm via the signal recognition particle pathway. J. Bacteriol. 185: 5706-5713. http://dx.doi .org/10.1128/JB.185.19.5706-5713.2003
    • (2003) J. Bacteriol , vol.185 , pp. 5706-5713
    • Schierle, C.F.1    Berkmen, M.2    Huber, D.3    Kumamoto, C.4    Boyd, D.5    Beckwith, J.6
  • 35
    • 1842561598 scopus 로고    scopus 로고
    • The organization of engaged and quiescent translocons in the endoplasmic reticulum of mammalian cells
    • Snapp, E.L., G.A. Reinhart, B.A. Bogert, J. Lippincott-Schwartz, and R.S. Hegde. 2004. The organization of engaged and quiescent translocons in the endoplasmic reticulum of mammalian cells. J. Cell Biol. 164: 997-1007. http://dx.doi.org/10.1083/jcb.200312079
    • (2004) J. Cell Biol , vol.164 , pp. 997-1007
    • Snapp, E.L.1    Reinhart, G.A.2    Bogert, B.A.3    Lippincott-Schwartz, J.4    Hegde, R.S.5
  • 38
    • 0242361323 scopus 로고    scopus 로고
    • MazF cleaves cellular mRNAs specifically at ACA to block protein synthesis in Escherichia coli
    • Zhang, Y., J. Zhang, K.P. Hoeflich, M. Ikura, G. Qing, and M. Inouye. 2003. MazF cleaves cellular mRNAs specifically at ACA to block protein synthesis in Escherichia coli. Mol. Cell. 12: 913-923. http://dx.doi .org/10.1016/S1097-2765(03)00402-7
    • (2003) Mol. Cell , vol.12 , pp. 913-923
    • Zhang, Y.1    Zhang, J.2    Hoeflich, K.P.3    Ikura, M.4    Qing, G.5    Inouye, M.6
  • 39
    • 54049111011 scopus 로고    scopus 로고
    • Structure of a complex of the ATPase SecA and the protein-translocation channel
    • Zimmer, J., Y. Nam, and T.A. Rapoport. 2008. Structure of a complex of the ATPase SecA and the protein-translocation channel. Nature. 455: 936-943. http://dx.doi.org/10.1038/nature07335
    • (2008) Nature , vol.455 , pp. 936-943
    • Zimmer, J.1    Nam, Y.2    Rapoport, T.A.3


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