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Volumn 367, Issue 1592, 2012, Pages 1016-1028

The bacterial Sec-translocase: Structure and mechanism

Author keywords

Membrane protein insertion; Protein translocation; SecA; SecY; Translocon

Indexed keywords

BACTERIUM; CYTOPLASM; MOLECULAR ANALYSIS; PROTEIN; SECRETION; TRANSLOCATION;

EID: 84858221348     PISSN: 09628436     EISSN: 14712970     Source Type: Journal    
DOI: 10.1098/rstb.2011.0201     Document Type: Review
Times cited : (126)

References (146)
  • 1
    • 0025297583 scopus 로고
    • The signal peptide
    • doi:10.1007/BF01868635
    • von Heijne, G. 1990 The signal peptide. J. Membr. Biol. 115, 195-201.(doi:10.1007/BF01868635)
    • (1990) J. Membr. Biol , vol.115 , pp. 195-201
    • von Heijne, G.1
  • 2
    • 0034602846 scopus 로고    scopus 로고
    • Discrimination between SRP- and SecA/SecBdependent substrates involves selective recognition of nascent chains by SRP and trigger factor
    • doi:10.1093/emboj/19.1.134
    • Beck, K., Wu, L. F., Brunner, J. & Muller, M. 2000 Discrimination between SRP- and SecA/SecBdependent substrates involves selective recognition of nascent chains by SRP and trigger factor. EMBO J. 19, 134-143.(doi:10.1093/emboj/19.1.134)
    • (2000) EMBO J , vol.19 , pp. 134-143
    • Beck, K.1    Wu, L.F.2    Brunner, J.3    Muller, M.4
  • 3
    • 33744925719 scopus 로고    scopus 로고
    • Sequence-specific interactions of nascent Escherichia coli polypeptides with trigger factor and signal recognition particle
    • Ullers, R. S., Houben, E. N., Brunner, J., Oudega, B., Harms, N. & Luirink, J. 2006 Sequence-specific interactions of nascent Escherichia coli polypeptides with trigger factor and signal recognition particle. J. Biol. Chem. 281, 13999-14005.
    • (2006) J. Biol. Chem , vol.281 , pp. 13999-14005
    • Ullers, R.S.1    Houben, E.N.2    Brunner, J.3    Oudega, B.4    Harms, N.5    Luirink, J.6
  • 4
    • 0020357598 scopus 로고
    • Protein translocation across the endoplasmic reticulum. I. Detection in the microsomal membrane of a receptor for the signal recognition particle
    • doi:10.1083/jcb.95.2.463
    • Gilmore, R., Blobel, G. & Walter, P. 1982 Protein translocation across the endoplasmic reticulum. I. Detection in the microsomal membrane of a receptor for the signal recognition particle. J. Cell Biol. 95, 463-469.(doi:10.1083/jcb.95.2.463)
    • (1982) J. Cell Biol , vol.95 , pp. 463-469
    • Gilmore, R.1    Blobel, G.2    Walter, P.3
  • 5
    • 0019822645 scopus 로고
    • Translocation of proteins across the endoplasmic reticulum. III. Signal recognition protein (SRP) causes signal sequencedependent and site-specific arrest of chain elongation that is released by microsomal membranes
    • doi:10.1083/jcb.91.2.557
    • Walter, P. & Blobel, G. 1981 Translocation of proteins across the endoplasmic reticulum. III. Signal recognition protein (SRP) causes signal sequencedependent and site-specific arrest of chain elongation that is released by microsomal membranes. J. Cell Biol. 91, 557-561.(doi:10.1083/jcb.91.2.557)
    • (1981) J. Cell Biol , vol.91 , pp. 557-561
    • Walter, P.1    Blobel, G.2
  • 6
    • 0024449598 scopus 로고
    • Three pure chaperone proteins of Escherichia coli-SecB, trigger factor and GroEL-form soluble complexes with precursor proteins in vitro
    • Lecker, S., Lill, R., Ziegelhoffer, T., Georgopoulos, C., Bassford Jr, P. J., Kumamoto, C. A. & Wickner, W. 1989 Three pure chaperone proteins of Escherichia coli-SecB, trigger factor and GroEL-form soluble complexes with precursor proteins in vitro. EMBO J. 8, 2703-2709.
    • (1989) EMBO J , vol.8 , pp. 2703-2709
    • Lecker, S.1    Lill, R.2    Ziegelhoffer, T.3    Georgopoulos, C.4    Bassford, P.J.5    Kumamoto, C.A.6    Wickner, W.7
  • 7
    • 0031037648 scopus 로고    scopus 로고
    • Binding of SecB to ribosome-bound polypeptides has the same characteristics as binding to full-length, denatured proteins
    • doi:10.1073/pnas.94.3.802
    • Randall, L. L., Topping, T. B., Hardy, S. J., Pavlov, M. Y., Freistroffer, D. V. & Ehrenberg, M. 1997 Binding of SecB to ribosome-bound polypeptides has the same characteristics as binding to full-length, denatured proteins. Proc. Natl Acad. Sci. USA 94, 802-807.(doi:10.1073/pnas.94.3.802)
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 802-807
    • Randall, L.L.1    Topping, T.B.2    Hardy, S.J.3    Pavlov, M.Y.4    Freistroffer, D.V.5    Ehrenberg, M.6
  • 8
    • 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, J. P., Schiebel, E., Driessen, A. J. & Wickner, W. 1990 The purified E. coli integral membrane protein SecY/E is sufficient for reconstitution of SecA-dependent precursor protein translocation. Cell 62, 649-657.(doi:10.1016/0092-8674(90)90111-Q)
    • (1990) Cell , vol.62 , pp. 649-657
    • Brundage, L.1    Hendrick, J.P.2    Schiebel, E.3    Driessen, A.J.4    Wickner, W.5
  • 10
    • 0028142465 scopus 로고
    • Reconstitution of an efficient protein translocation machinery comprising SecA and the three membrane proteins, SecY, SecE, and SecG (p12)
    • Hanada, M., Nishiyama, K. I., Mizushima, S. & Tokuda, H. 1994 Reconstitution of an efficient protein translocation machinery comprising SecA and the three membrane proteins, SecY, SecE, and SecG (p12). J. Biol. Chem. 269, 23625-23631.
    • (1994) J. Biol. Chem , vol.269 , pp. 23625-23631
    • Hanada, M.1    Nishiyama, K.I.2    Mizushima, S.3    Tokuda, H.4
  • 11
    • 0028241570 scopus 로고
    • Disruption of the gene encoding p12 (SecG) reveals the direct involvement and important function of SecG in the protein translocation of Escherichia coli at low temperature
    • Nishiyama, K., Hanada, M. & Tokuda, H. 1994 Disruption of the gene encoding p12 (SecG) reveals the direct involvement and important function of SecG in the protein translocation of Escherichia coli at low temperature. EMBO J. 13, 3272-3277.
    • (1994) EMBO J , vol.13 , pp. 3272-3277
    • Nishiyama, K.1    Hanada, M.2    Tokuda, H.3
  • 12
    • 0027217073 scopus 로고
    • A novel membrane protein involved in protein translocation across the cytoplasmic membrane of Escherichia coli
    • Nishiyama, K., Mizushima, S. & Tokuda, H. 1993 A novel membrane protein involved in protein translocation across the cytoplasmic membrane of Escherichia coli. EMBO J. 12, 3409-3415.
    • (1993) EMBO J , vol.12 , pp. 3409-3415
    • Nishiyama, K.1    Mizushima, S.2    Tokuda, H.3
  • 13
    • 0030029447 scopus 로고    scopus 로고
    • SecG plays a critical role in protein translocation in the absence of the proton motive force as well as at low temperature
    • doi:10.1016/0014-5793(96)00066-X
    • Hanada, M., Nishiyama, K. & Tokuda, H. 1996 SecG plays a critical role in protein translocation in the absence of the proton motive force as well as at low temperature. FEBS Lett. 381, 25-28.(doi:10.1016/0014-5793(96)00066-X)
    • (1996) FEBS Lett , vol.381 , pp. 25-28
    • Hanada, M.1    Nishiyama, K.2    Tokuda, H.3
  • 14
    • 0035108130 scopus 로고    scopus 로고
    • SecG function and phospholipid metabolism in Escherichia coli
    • doi:10.1128/JB.183.6.2006-2012.2001
    • Flower, A. M. 2001 SecG function and phospholipid metabolism in Escherichia coli. J. Bacteriol. 183, 2006-2012.(doi:10.1128/JB.183.6.2006-2012.2001)
    • (2001) J. Bacteriol , vol.183 , pp. 2006-2012
    • Flower, A.M.1
  • 15
    • 0033694344 scopus 로고    scopus 로고
    • Both transmembrane domains of SecG contribute to signal sequence recognition by the Escherichia coli protein export machinery
    • doi:10.1046/j.1365-2958.2000.02153.x
    • Bost, S., Silva, F., Rudaz, C. & Belin, D. 2000 Both transmembrane domains of SecG contribute to signal sequence recognition by the Escherichia coli protein export machinery. Mol. Microbiol. 38, 575-587.(doi:10.1046/j.1365-2958.2000.02153.x)
    • (2000) Mol. Microbiol , vol.38 , pp. 575-587
    • Bost, S.1    Silva, F.2    Rudaz, C.3    Belin, D.4
  • 16
    • 0033833862 scopus 로고    scopus 로고
    • SecG is an auxiliary component of the protein export apparatus of Escherichia coli
    • doi:10.1007/s004380050039
    • Flower, A. M., Hines, L. L. & Pfennig, P. L. 2000 SecG is an auxiliary component of the protein export apparatus of Escherichia coli. Mol. Gen. Genet. 263, 131-136.(doi:10.1007/s004380050039)
    • (2000) Mol. Gen. Genet , vol.263 , pp. 131-136
    • Flower, A.M.1    Hines, L.L.2    Pfennig, P.L.3
  • 17
    • 0030949334 scopus 로고    scopus 로고
    • Subunit interactions in the Escherichia coli protein translocase: SecE and SecG associate independently with SecY
    • doi:10.1016/S0014-5793(97)00376-1
    • Homma, T., Yoshihisa, T. & Ito, K. 1997 Subunit interactions in the Escherichia coli protein translocase: SecE and SecG associate independently with SecY. FEBS Lett. 408, 11-15.(doi:10.1016/S0014-5793(97)00376-1)
    • (1997) FEBS Lett , vol.408 , pp. 11-15
    • Homma, T.1    Yoshihisa, T.2    Ito, K.3
  • 18
    • 2942517660 scopus 로고    scopus 로고
    • Mutational analysis of transmembrane regions 3 and 4 of SecY, a central component of protein translocase
    • doi:10.1128/JB.186.12.3960-3969.2004
    • Mori, H., Shimokawa, N., Satoh, Y. & Ito, K. 2004 Mutational analysis of transmembrane regions 3 and 4 of SecY, a central component of protein translocase. J. Bacteriol. 186, 3960-3969.(doi:10.1128/JB.186.12.3960-3969.2004)
    • (2004) J. Bacteriol , vol.186 , pp. 3960-3969
    • Mori, H.1    Shimokawa, N.2    Satoh, Y.3    Ito, K.4
  • 19
    • 0038408667 scopus 로고    scopus 로고
    • Nearest neighbor analysis of the SecYEG complex. I. Identification of a SecY-SecG interface
    • doi:10.1021/bi034331a
    • Satoh, Y., Matsumoto, G., Mori, H. & Ito, K. 2003 Nearest neighbor analysis of the SecYEG complex. I. Identification of a SecY-SecG interface. Biochemistry 42, 7434-7441.(doi:10.1021/bi034331a)
    • (2003) Biochemistry , vol.42 , pp. 7434-7441
    • Satoh, Y.1    Matsumoto, G.2    Mori, H.3    Ito, K.4
  • 20
    • 0037063356 scopus 로고    scopus 로고
    • SecY-SecY and SecY-SecG contacts revealed by sitespecific crosslinking
    • doi:10.1016/S0014-5793(02)03202-7
    • van der Sluis, E. O., Nouwen, N. & Driessen, A. J. 2002 SecY-SecY and SecY-SecG contacts revealed by sitespecific crosslinking. FEBS Lett. 527, 159-165.(doi:10.1016/S0014-5793(02)03202-7)
    • (2002) FEBS Lett , vol.527 , pp. 159-165
    • van der Sluis, E.O.1    Nouwen, N.2    Driessen, A.J.3
  • 21
    • 0142039007 scopus 로고    scopus 로고
    • Depletion of SecDF-YajC causes a decrease in the level of SecG: Implication for their functional interaction
    • doi:10.1016/S0014-5793(03)00847-0
    • Kato, Y., Nishiyama, K. & Tokuda, H. 2003 Depletion of SecDF-YajC causes a decrease in the level of SecG: implication for their functional interaction. FEBS Lett. 550, 114-118.(doi:10.1016/S0014-5793(03)00847-0)
    • (2003) FEBS Lett , vol.550 , pp. 114-118
    • Kato, Y.1    Nishiyama, K.2    Tokuda, H.3
  • 22
    • 0030959069 scopus 로고    scopus 로고
    • Distinct catalytic roles of the SecYE, SecG and SecDFyajC subunits of preprotein translocase holoenzyme
    • doi:10.1093/emboj/16.10.2756
    • Duong, F. & Wickner, W. 1997 Distinct catalytic roles of the SecYE, SecG and SecDFyajC subunits of preprotein translocase holoenzyme. EMBO J. 16, 2756-2768.(doi:10.1093/emboj/16.10.2756)
    • (1997) EMBO J , vol.16 , pp. 2756-2768
    • Duong, F.1    Wickner, W.2
  • 23
    • 35748932922 scopus 로고    scopus 로고
    • Topology inversion of SecG is essential for cytosolic SecA-dependent stimulation of protein translocation
    • doi:10.1074/jbc.m704716200
    • Sugai, R., Takemae, K., Tokuda, H. & Nishiyama, K. 2007 Topology inversion of SecG is essential for cytosolic SecA-dependent stimulation of protein translocation. J. Biol. Chem. 282, 29540-29548.(doi:10.1074/jbc.m704716200)
    • (2007) J. Biol. Chem , vol.282 , pp. 29540-29548
    • Sugai, R.1    Takemae, K.2    Tokuda, H.3    Nishiyama, K.4
  • 24
    • 0036775559 scopus 로고    scopus 로고
    • Membrane topology inversion of SecG detected by labeling with a membrane-impermeable sulfhydryl reagent that causes a close association of SecG with SecA
    • Nagamori, S., Nishiyama, K. & Tokuda, H. 2002 Membrane topology inversion of SecG detected by labeling with a membrane-impermeable sulfhydryl reagent that causes a close association of SecG with SecA. J. Biochem. 132, 629-634.
    • (2002) J. Biochem , vol.132 , pp. 629-634
    • Nagamori, S.1    Nishiyama, K.2    Tokuda, H.3
  • 25
    • 0029997381 scopus 로고    scopus 로고
    • Inversion of the membrane topology of SecG coupled with SecAdependent preprotein translocation
    • doi:10.1016/S0092-8674(00)81083-1
    • Nishiyama, K., Suzuki, T. & Tokuda, H. 1996 Inversion of the membrane topology of SecG coupled with SecAdependent preprotein translocation. Cell 85, 71-81.(doi:10.1016/S0092-8674(00)81083-1)
    • (1996) Cell , vol.85 , pp. 71-81
    • Nishiyama, K.1    Suzuki, T.2    Tokuda, H.3
  • 26
    • 0032506216 scopus 로고    scopus 로고
    • Roles of SecG in ATP- and SecA-dependent protein translocation
    • doi:10. 1073/pnas.95.23.13567
    • Matsumoto, G., Mori, H. & Ito, K. 1998 Roles of SecG in ATP- and SecA-dependent protein translocation. Proc. Natl Acad. Sci. USA 95, 13567-13572.(doi:10. 1073/pnas.95.23.13567)
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 13567-13572
    • Matsumoto, G.1    Mori, H.2    Ito, K.3
  • 28
    • 0031820398 scopus 로고    scopus 로고
    • Amino-terminal region of SecA is involved in the function of SecG for protein translocation into Escherichia coli membrane vesicles
    • Mori, H., Sugiyama, H., Yamanaka, M., Sato, K., Tagaya, M. & Mizushima, S. 1998 Amino-terminal region of SecA is involved in the function of SecG for protein translocation into Escherichia coli membrane vesicles. J. Biochem. 124, 122-129.
    • (1998) J. Biochem , vol.124 , pp. 122-129
    • Mori, H.1    Sugiyama, H.2    Yamanaka, M.3    Sato, K.4    Tagaya, M.5    Mizushima, S.6
  • 29
    • 0031596299 scopus 로고    scopus 로고
    • Coupled structure changes of SecA and SecG revealed by the synthetic lethality of the secAcsR11 and delta secG: Kan double mutant
    • doi:10.1046/j.1365-2958.1998.00937.x
    • Suzuki, H., Nishiyama, K. & Tokuda, H. 1998 Coupled structure changes of SecA and SecG revealed by the synthetic lethality of the secAcsR11 and delta secG: kan double mutant. Mol. Microbiol. 29, 331-341.(doi:10. 1046/j.1365-2958.1998.00937.x)
    • (1998) Mol. Microbiol , vol.29 , pp. 331-341
    • Suzuki, H.1    Nishiyama, K.2    Tokuda, H.3
  • 30
    • 54049111011 scopus 로고    scopus 로고
    • Structure of a complex of the ATPase SecA and the protein-translocation channel
    • doi:10.1038/nature07335
    • Zimmer, J., Nam, Y. & Rapoport, T. A. 2008 Structure of a complex of the ATPase SecA and the protein-translocation channel. Nature 455, 936-943.(doi:10.1038/nature07335)
    • (2008) Nature , vol.455 , pp. 936-943
    • Zimmer, J.1    Nam, Y.2    Rapoport, T.A.3
  • 31
    • 79953302604 scopus 로고    scopus 로고
    • Mapping of the SecA.SecY and SecA.SecG interfaces by site-directed in vivo photocross- linking
    • Das, S. & Oliver, D. B. 2011 Mapping of the SecA.SecY and SecA.SecG interfaces by site-directed in vivo photocross- linking. J. Biol. Chem. 286, 12371-12380.
    • (2011) J. Biol. Chem , vol.286 , pp. 12371-12380
    • Das, S.1    Oliver, D.B.2
  • 32
    • 33845999952 scopus 로고    scopus 로고
    • The long alpha-helix of SecA is important for the ATPase coupling of translocation
    • Mori, H. & Ito, K. 2006 The long alpha-helix of SecA is important for the ATPase coupling of translocation. J. Biol. Chem. 281, 36249-36256.
    • (2006) J. Biol. Chem , vol.281 , pp. 36249-36256
    • Mori, H.1    Ito, K.2
  • 33
    • 0026073130 scopus 로고
    • Purification of SecE and reconstitution of SecE-dependent protein translocation activity
    • doi:10.1016/0014-5793(91)80156-W
    • Tokuda, H., Akimaru, J., Matsuyama, S., Nishiyama, K. & Mizushima, S. 1991 Purification of SecE and reconstitution of SecE-dependent protein translocation activity. FEBS Lett. 279, 233-236.(doi:10.1016/0014-5793(91)80156-W)
    • (1991) FEBS Lett , vol.279 , pp. 233-236
    • Tokuda, H.1    Akimaru, J.2    Matsuyama, S.3    Nishiyama, K.4    Mizushima, S.5
  • 34
    • 0026688434 scopus 로고
    • The carboxyl-terminal region of SecE interacts with SecY and is functional in the reconstitution of protein translocation activity in Escherichia coli
    • Nishiyama, K., Mizushima, S. & Tokuda, H. 1992 The carboxyl-terminal region of SecE interacts with SecY and is functional in the reconstitution of protein translocation activity in Escherichia coli. J. Biol. Chem. 267, 7170-7176.
    • (1992) J. Biol. Chem , vol.267 , pp. 7170-7176
    • Nishiyama, K.1    Mizushima, S.2    Tokuda, H.3
  • 35
    • 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., Bieker, K. L., Ottemann, K. M., Silhavy, T. J. & Beckwith, J. 1991 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) EMBO J , vol.10 , pp. 1749-1757
    • Schatz, P.J.1    Bieker, K.L.2    Ottemann, K.M.3    Silhavy, T.J.4    Beckwith, J.5
  • 36
    • 0037427963 scopus 로고    scopus 로고
    • The general protein secretory pathway: Phylogenetic analyses leading to evolutionary conclusions
    • doi:10.1016/S0005-2736(02)00662-4
    • Cao, T. B. & Saier Jr, M. H. 2003 The general protein secretory pathway: phylogenetic analyses leading to evolutionary conclusions. Biochim. Biophys. Acta 1609, 115-125.(doi:10.1016/S0005-2736(02)00662-4)
    • (2003) Biochim. Biophys. Acta , vol.1609 , pp. 115-125
    • Cao, T.B.1    Saier, M.H.2
  • 37
    • 0028334912 scopus 로고
    • Residues essential for the function of SecE, a membrane component of the Escherichia coli secretion apparatus, are located in a conserved cytoplasmic region
    • doi:10.1073/pnas.91.7.2557
    • Murphy, C. K. & Beckwith, J. 1994 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. USA 91, 2557-2561.(doi:10.1073/pnas.91.7.2557)
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 2557-2561
    • Murphy, C.K.1    Beckwith, J.2
  • 38
    • 0029810616 scopus 로고    scopus 로고
    • In vivo analyses of interactions between SecE and SecY, core components of the Escherichia coli protein translocation machinery
    • Pohlschroder, M., Murphy, C. & Beckwith, J. 1996 In vivo analyses of interactions between SecE and SecY, core components of the Escherichia coli protein translocation machinery. J. Biol. Chem. 271, 19908-19914.
    • (1996) J. Biol. Chem , vol.271 , pp. 19908-19914
    • Pohlschroder, M.1    Murphy, C.2    Beckwith, J.3
  • 39
    • 0029017127 scopus 로고
    • FtsH is required for proteolytic elimination of uncomplexed forms of SecY, an essential protein translocase subunit
    • doi:10.1073/pnas.92.10.4532
    • Kihara, A., Akiyama, Y. & Ito, K. 1995 FtsH is required for proteolytic elimination of uncomplexed forms of SecY, an essential protein translocase subunit. Proc. Natl Acad. Sci. USA 92, 4532-4536.(doi:10.1073/pnas.92.10.4532)
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 4532-4536
    • Kihara, A.1    Akiyama, Y.2    Ito, K.3
  • 40
    • 59649110315 scopus 로고    scopus 로고
    • The roles of pore ring and plug in the SecY protein-conducting channel
    • doi:10.1085/jgp.200810062
    • Gumbart, J. & Schulten, K. 2008 The roles of pore ring and plug in the SecY protein-conducting channel. J. Gen. Physiol. 132, 709-719.(doi:10.1085/jgp.200810062)
    • (2008) J. Gen. Physiol , vol.132 , pp. 709-719
    • Gumbart, J.1    Schulten, K.2
  • 41
    • 34248563028 scopus 로고    scopus 로고
    • Determining the conductance of the SecY protein translocation channel for small molecules
    • doi:10.1016/j.molcel.2007.03.022
    • Saparov, S. M., Erlandson, K., Cannon, K., Schaletzky, J., Schulman, S., Rapoport, T. A. & Pohl, P. 2007 Determining the conductance of the SecY protein translocation channel for small molecules. Mol. Cell 26, 501-509.(doi:10.1016/j.molcel.2007.03.022)
    • (2007) Mol. Cell , vol.26 , pp. 501-509
    • Saparov, S.M.1    Erlandson, K.2    Cannon, K.3    Schaletzky, J.4    Schulman, S.5    Rapoport, T.A.6    Pohl, P.7
  • 42
    • 79955901001 scopus 로고    scopus 로고
    • Preserving the membrane barrier for small molecules during bacterial protein translocation
    • doi:10. 1038/nature10014
    • Park, E. & Rapoport, T. A. 2011 Preserving the membrane barrier for small molecules during bacterial protein translocation. Nature 473, 239-242.(doi:10. 1038/nature10014)
    • (2011) Nature , vol.473 , pp. 239-242
    • Park, E.1    Rapoport, T.A.2
  • 43
    • 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, B. M., Stirling, C. J. & Rapoport, T. A. 1998 Signal sequence recognition in posttranslational protein transport across the yeast ER membrane. Cell 94, 795-807.(doi:10.1016/S0092-8674(00)81738-9)
    • (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
  • 44
    • 0346099350 scopus 로고    scopus 로고
    • Interactions between Sec complex and prepro-alpha-factor during posttranslational protein transport into the endoplasmic reticulum
    • doi:10.1091/mbc.E03-06-0390
    • Plath, K., Wilkinson, B. M., Stirling, C. J. & Rapoport, T. A. 2004 Interactions between Sec complex and prepro-alpha-factor during posttranslational protein transport into the endoplasmic reticulum. Mol. Biol. Cell 15, 1-10.(doi:10.1091/mbc.E03-06-0390)
    • (2004) Mol. Biol. Cell , vol.15 , pp. 1-10
    • Plath, K.1    Wilkinson, B.M.2    Stirling, C.J.3    Rapoport, T.A.4
  • 45
    • 85027919032 scopus 로고    scopus 로고
    • Cryo-EM structure of the ribosome-SecYE complex in the membrane environment
    • doi:10. 1038/nsmb.2026
    • Frauenfeld, J. et al. 2011 Cryo-EM structure of the ribosome-SecYE complex in the membrane environment. Nat. Struct. Mol. Biol. 18, 614-621.(doi:10. 1038/nsmb.2026)
    • (2011) Nat. Struct. Mol. Biol , vol.18 , pp. 614-621
    • Frauenfeld, J.1
  • 46
    • 37349107850 scopus 로고    scopus 로고
    • Ribosome binding of a single copy of the SecY complex: Implications for protein translocation
    • doi:10.1016/j.molcel.2007.10.034
    • Menetret, J. F. et al. 2007 Ribosome binding of a single copy of the SecY complex: implications for protein translocation. Mol. Cell 28, 1083-1092.(doi:10.1016/j.molcel.2007.10.034)
    • (2007) Mol. Cell , vol.28 , pp. 1083-1092
    • Menetret, J.F.1
  • 47
    • 54049151196 scopus 로고    scopus 로고
    • Conformational transition of Sec machinery inferred from bacterial SecYE structures
    • doi:10.1038/nature07421
    • Tsukazaki, T. et al. 2008 Conformational transition of Sec machinery inferred from bacterial SecYE structures. Nature 455, 988-991.(doi:10.1038/nature07421)
    • (2008) Nature , vol.455 , pp. 988-991
    • Tsukazaki, T.1
  • 48
    • 33750844195 scopus 로고    scopus 로고
    • Different modes of SecY-SecA interactions revealed by site-directed in vivo photocross-linking
    • doi:10.1073/pnas.0606390103
    • Mori, H. & Ito, K. 2006 Different modes of SecY-SecA interactions revealed by site-directed in vivo photocross-linking. Proc. Natl Acad. Sci. USA 103, 16159-16164.(doi:10.1073/pnas.0606390103)
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 16159-16164
    • Mori, H.1    Ito, K.2
  • 49
    • 33746905934 scopus 로고    scopus 로고
    • Identification of two interaction sites in SecY that are important for the functional interaction with SecA
    • doi:10.1016/j.jmb.2006.07.017
    • van der Sluis, E. O., Nouwen, N., Koch, J., de Keyzer, J., van der Does, C., Tampe, R. & Driessen, A. J. 2006 Identification of two interaction sites in SecY that are important for the functional interaction with SecA. J. Mol. Biol. 361, 839-849.(doi:10.1016/j.jmb.2006.07.017)
    • (2006) J. Mol. Biol , vol.361 , pp. 839-849
    • van der Sluis, E.O.1    Nouwen, N.2    Koch, J.3    de Keyzer, J.4    van der Does, C.5    Tampe, R.6    Driessen, A.J.7
  • 50
    • 78049253482 scopus 로고    scopus 로고
    • Lateral opening of a translocon upon entry of protein suggests the mechanism of insertion into membranes
    • doi:10.1073/pnas.1012556107
    • Egea, P. F. & Stroud, R. M. 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.(doi:10.1073/pnas.1012556107)
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 17182-17187
    • Egea, P.F.1    Stroud, R.M.2
  • 51
    • 34848895197 scopus 로고    scopus 로고
    • Structural determinants of lateral gate opening in the protein translocon
    • doi:10.1021/bi700835d
    • Gumbart, J. & Schulten, K. 2007 Structural determinants of lateral gate opening in the protein translocon. Biochemistry 46, 11147-11157.(doi:10.1021/bi700835d)
    • (2007) Biochemistry , vol.46 , pp. 11147-11157
    • Gumbart, J.1    Schulten, K.2
  • 52
    • 67650173024 scopus 로고    scopus 로고
    • The lateral gate of SecYEG opens during protein translocation
    • doi:10.1074/jbc.M901855200
    • du Plessis, D. J., Berrelkamp, G., Nouwen, N. & Driessen, A. J. 2009 The lateral gate of SecYEG opens during protein translocation. J. Biol. Chem. 284, 15805-15814.(doi:10.1074/jbc.M901855200)
    • (2009) J. Biol. Chem , vol.284 , pp. 15805-15814
    • du Plessis, D.J.1    Berrelkamp, G.2    Nouwen, N.3    Driessen, A.J.4
  • 53
    • 77957347075 scopus 로고    scopus 로고
    • Light-induced control of protein translocation by the SecYEG complex
    • doi:10.1002/anie.201002243
    • Bonardi, F., London, G., Nouwen, N., Feringa, B. L. & Driessen, A. J. 2010 Light-induced control of protein translocation by the SecYEG complex. Angew. Chem. Int. Ed Engl. 49, 7234-7238.(doi:10.1002/anie.201002243)
    • (2010) Angew. Chem. Int. Ed Engl , vol.49 , pp. 7234-7238
    • Bonardi, F.1    London, G.2    Nouwen, N.3    Feringa, B.L.4    Driessen, A.J.5
  • 54
    • 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.(doi:10.1091/mbc.E06-03-0200)
    • (2006) Mol. Biol. Cell , vol.17 , pp. 4063-4068
    • Junne, T.1    Schwede, T.2    Goder, V.3    Spiess, M.4
  • 55
    • 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
    • Li, W., Schulman, S., Boyd, D., Erlandson, K., Beckwith, J. & Rapoport, T. A. 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.(doi:10.1016/j.molcel.2007.05.002)
    • (2007) Mol. Cell , vol.26 , pp. 511-521
    • Li, W.1    Schulman, S.2    Boyd, D.3    Erlandson, K.4    Beckwith, J.5    Rapoport, T.A.6
  • 56
    • 33847698213 scopus 로고    scopus 로고
    • Deregulation of the SecYEG translocation channel upon removal of the plug domain
    • doi:10.1074/jbc.M610060200
    • Maillard, A. P., Lalani, S., Silva, F., Belin, D. & Duong, F. 2007 Deregulation of the SecYEG translocation channel upon removal of the plug domain. J. Biol. Chem. 282, 1281-1287.(doi:10.1074/jbc.M610060200)
    • (2007) J. Biol. Chem , vol.282 , pp. 1281-1287
    • Maillard, A.P.1    Lalani, S.2    Silva, F.3    Belin, D.4    Duong, F.5
  • 57
    • 0033032483 scopus 로고    scopus 로고
    • Mapping an interface of SecY (PrlA) and SecE (PrlG) by using synthetic phenotypes and in vivo cross-linking
    • Harris, C. R. & Silhavy, T. J. 1999 Mapping an interface of SecY (PrlA) and SecE (PrlG) by using synthetic phenotypes and in vivo cross-linking. J. Bacteriol. 181, 3438-3444.
    • (1999) J. Bacteriol , vol.181 , pp. 3438-3444
    • Harris, C.R.1    Silhavy, T.J.2
  • 58
    • 27144525002 scopus 로고    scopus 로고
    • Investigating the SecY plug movement at the SecYEG translocation channel
    • doi:10.1038/sj.emboj.7600804
    • Tam, P. C., Maillard, A. P., Chan, K. K. & Duong, F. 2005 Investigating the SecY plug movement at the SecYEG translocation channel. EMBO J. 24, 3380-3388.(doi:10.1038/sj.emboj.7600804)
    • (2005) EMBO J , vol.24 , pp. 3380-3388
    • Tam, P.C.1    Maillard, A.P.2    Chan, K.K.3    Duong, F.4
  • 59
    • 77954912142 scopus 로고    scopus 로고
    • Immobilization of the plug domain inside the SecY channel allows unrestricted protein translocation
    • doi:10.1074/jbc.M110.124636
    • Lycklama a Nijeholt, J. A., Bulacu, M., Marrink, S. J. & Driessen, A. J. 2010 Immobilization of the plug domain inside the SecY channel allows unrestricted protein translocation. J. Biol. Chem. 285, 23747-23754.(doi:10.1074/jbc.M110.124636)
    • (2010) J. Biol. Chem , vol.285 , pp. 23747-23754
    • Lycklamaa, N.J.A.1    Bulacu, M.2    Marrink, S.J.3    Driessen, A.J.4
  • 60
    • 77950448361 scopus 로고    scopus 로고
    • Hydrophobically stabilized open state for the lateral gate of the Sec translocon
    • doi:10.1073/pnas.0914752107
    • Zhang, B. & Miller III, T. F. 2010 Hydrophobically stabilized open state for the lateral gate of the Sec translocon. Proc. Natl Acad. Sci. USA 107, 5399-5404.(doi:10.1073/pnas.0914752107)
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 5399-5404
    • Zhang, B.1    Miller, T.F.2
  • 61
    • 83755168976 scopus 로고    scopus 로고
    • Conformational dynamics of the plug domain of the SecYEG protein-conducting channel
    • doi:10.1074/jbc.M111.297507
    • Lycklama a Nijeholt, J. A., Wu, Z. C. & Driessen, A. J. 2011 Conformational dynamics of the plug domain of the SecYEG protein-conducting channel. J. Biol. Chem. 286, 43881-43890.(doi:10.1074/jbc.M111.297507)
    • (2011) J. Biol. Chem , vol.286 , pp. 43881-43890
    • Lycklamaa, N.J.A.1    Wu, Z.C.2    Driessen, A.J.3
  • 62
    • 0020390269 scopus 로고
    • Mechanism of incorporation of cell envelope proteins in Escherichia coli
    • doi:10.1146/annurev.mi.36.100182.002251
    • Michaelis, S. & Beckwith, J. 1982 Mechanism of incorporation of cell envelope proteins in Escherichia coli. Annu. Rev. Microbiol. 36, 435-465.(doi:10.1146/annurev.mi.36.100182.002251)
    • (1982) Annu. Rev. Microbiol , vol.36 , pp. 435-465
    • Michaelis, S.1    Beckwith, J.2
  • 63
    • 0021401874 scopus 로고
    • A defined mutation in the protein export gene within the spc ribosomal protein operon of Escherichia coli: Isolation and characterization of a new temperaturesensitive secY mutant
    • Shiba, K., Ito, K., Yura, T. & Cerretti, D. P. 1984 A defined mutation in the protein export gene within the spc ribosomal protein operon of Escherichia coli: isolation and characterization of a new temperaturesensitive secY mutant. EMBO J. 3, 631-635.
    • (1984) EMBO J , vol.3 , pp. 631-635
    • Shiba, K.1    Ito, K.2    Yura, T.3    Cerretti, D.P.4
  • 64
    • 0029111417 scopus 로고
    • A new genetic selection identifies essential residues in SecG, a component of the Escherichia coli protein export machinery
    • Bost, S. & Belin, D. 1995 A new genetic selection identifies essential residues in SecG, a component of the Escherichia coli protein export machinery. EMBO J. 14, 4412-4421.
    • (1995) EMBO J , vol.14 , pp. 4412-4421
    • Bost, S.1    Belin, D.2
  • 65
    • 0027457077 scopus 로고
    • A signal sequence is not required for protein export in prlA mutants of Escherichia coli
    • Derman, A. I., Puziss, J. W., Bassford Jr, P. J. & Beckwith, J. 1993 A signal sequence is not required for protein export in prlA mutants of Escherichia coli. EMBO J. 12, 879-888.
    • (1993) EMBO J , vol.12 , pp. 879-888
    • Derman, A.I.1    Puziss, J.W.2    Bassford, P.J.3    Beckwith, J.4
  • 66
    • 0019381724 scopus 로고
    • Suppressor mutations that restore export of a protein with a defective signal sequence
    • doi:10.1016/0092-8674(81)90272-5
    • Emr, S. D., Hanley-Way, S. & Silhavy, T. J. 1981 Suppressor mutations that restore export of a protein with a defective signal sequence. Cell 23, 79-88.(doi:10.1016/0092-8674(81)90272-5)
    • (1981) Cell , vol.23 , pp. 79-88
    • Emr, S.D.1    Hanley-Way, S.2    Silhavy, T.J.3
  • 67
    • 0028102530 scopus 로고
    • PrlA and PrlG suppressors reduce the requirement for signal sequence recognition
    • Flower, A. M., Doebele, R. C. & Silhavy, T. J. 1994 PrlA and PrlG suppressors reduce the requirement for signal sequence recognition. J. Bacteriol. 176, 5607-5614.
    • (1994) J. Bacteriol , vol.176 , pp. 5607-5614
    • Flower, A.M.1    Doebele, R.C.2    Silhavy, T.J.3
  • 68
    • 24944465005 scopus 로고    scopus 로고
    • Modeling the effects of prl mutations on the Escherichia coli SecY complex
    • doi:10.1128/JB.187.18.6454-6465.2005
    • Smith, M. A., Clemons Jr, W. M., DeMars, C. J. & Flower, A. M. 2005 Modeling the effects of prl mutations on the Escherichia coli SecY complex. J. Bacteriol. 187, 6454-6465.(doi:10.1128/JB.187.18.6454-6465.2005)
    • (2005) J. Bacteriol , vol.187 , pp. 6454-6465
    • Smith, M.A.1    Clemons, W.M.2    Demars, C.J.3    Flower, A.M.4
  • 69
    • 0028925920 scopus 로고
    • The allele-specific synthetic lethality of prlA-prlG double mutants predicts interactive domains of SecY and SecE
    • Flower, A. M., Osborne, R. S. & Silhavy, T. J. 1995 The allele-specific synthetic lethality of prlA-prlG double mutants predicts interactive domains of SecY and SecE. EMBO J. 14, 884-893.
    • (1995) EMBO J , vol.14 , pp. 884-893
    • Flower, A.M.1    Osborne, R.S.2    Silhavy, T.J.3
  • 70
    • 0027219902 scopus 로고
    • PrlA suppressor mutations cluster in regions corresponding to three distinct topological domains
    • Osborne, R. S. & Silhavy, T. J. 1993 PrlA suppressor mutations cluster in regions corresponding to three distinct topological domains. EMBO J. 12, 3391-3398.
    • (1993) EMBO J , vol.12 , pp. 3391-3398
    • Osborne, R.S.1    Silhavy, T.J.2
  • 71
    • 0032125782 scopus 로고    scopus 로고
    • PrlA4 prevents the rejection of signal sequence defective preproteins by stabilizing the SecA-SecY interaction during the initiation of translocation
    • doi:10.1093/emboj/17.13.3631
    • van der Wolk, J. P., Fekkes, P., Boorsma, A., Huie, J. L., Silhavy, T. J. & Driessen, A. J. 1998 PrlA4 prevents the rejection of signal sequence defective preproteins by stabilizing the SecA-SecY interaction during the initiation of translocation. EMBO J. 17, 3631-3639.(doi:10.1093/emboj/17.13.3631)
    • (1998) EMBO J , vol.17 , pp. 3631-3639
    • van der Wolk, J.P.1    Fekkes, P.2    Boorsma, A.3    Huie, J.L.4    Silhavy, T.J.5    Driessen, A.J.6
  • 72
    • 77954635029 scopus 로고    scopus 로고
    • Dynamics of SecY translocons with translocation-defective mutations
    • doi:10.1016/j.str.2010.04.010
    • Bondar, A. N., del Val, C., Freites, J. A., Tobias, D. J. & White, S. H. 2010 Dynamics of SecY translocons with translocation-defective mutations. Structure 18, 847-857.(doi:10.1016/j.str.2010.04.010)
    • (2010) Structure , vol.18 , pp. 847-857
    • Bondar, A.N.1    del Val, C.2    Freites, J.A.3    Tobias, D.J.4    White, S.H.5
  • 73
    • 0030013237 scopus 로고    scopus 로고
    • PrlA suppressors in Escherichia coli relieve the proton electrochemical gradient dependency of translocation of wild-type precursors
    • doi:10.1073/pnas.93.12.5953
    • Nouwen, N., de Kruijff, B. & Tommassen, J. 1996 PrlA suppressors in Escherichia coli relieve the proton electrochemical gradient dependency of translocation of wild-type precursors. Proc. Natl Acad. Sci. USA 93, 5953-5957.(doi:10.1073/pnas.93.12.5953)
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 5953-5957
    • Nouwen, N.1    de Kruijff, B.2    Tommassen, J.3
  • 74
    • 79956359999 scopus 로고    scopus 로고
    • Probing the SecYEG translocation pore size with preproteins conjugated with sizable rigid spherical molecules
    • doi:10.1073/pnas.1101705108
    • Bonardi, F., Halza, E., Walko, M., Du Plessis, F., Nouwen, N., Feringa, B. L. & Driessen, A. J. 2011 Probing the SecYEG translocation pore size with preproteins conjugated with sizable rigid spherical molecules. Proc. Natl Acad. Sci. USA 108, 7775-7780.(doi:10.1073/pnas.1101705108)
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 7775-7780
    • Bonardi, F.1    Halza, E.2    Walko, M.3    du Plessis, F.4    Nouwen, N.5    Feringa, B.L.6    Driessen, A.J.7
  • 75
    • 70450171353 scopus 로고    scopus 로고
    • Signal peptides are allosteric activators of the protein translocase
    • doi:10.1038/nature08559
    • Gouridis, G., Karamanou, S., Gelis, I., Kalodimos, C. G. & Economou, A. 2009 Signal peptides are allosteric activators of the protein translocase. Nature 462, 363-367.(doi:10.1038/nature08559)
    • (2009) Nature , vol.462 , pp. 363-367
    • Gouridis, G.1    Karamanou, S.2    Gelis, I.3    Kalodimos, C.G.4    Economou, A.5
  • 76
    • 0025036708 scopus 로고
    • The binding cascade of SecB to SecA to SecY/E mediates preprotein targeting to the E. coli plasma membrane
    • doi:10.1016/0092-8674(90)90160-G
    • Hartl, F. U., Lecker, S., Schiebel, E., Hendrick, J. P. & Wickner, W. 1990 The binding cascade of SecB to SecA to SecY/E mediates preprotein targeting to the E. coli plasma membrane. Cell 63, 269-279.(doi:10.1016/0092-8674(90)90160-G)
    • (1990) Cell , vol.63 , pp. 269-279
    • Hartl, F.U.1    Lecker, S.2    Schiebel, E.3    Hendrick, J.P.4    Wickner, W.5
  • 77
    • 0025019705 scopus 로고
    • The ATPase activity of SecA is regulated by acidic phospholipids, SecY, and the leader and mature domains of precursor proteins
    • doi:10.1016/0092-8674(90)90742-W
    • Lill, R., Dowhan, W. & Wickner, W. 1990 The ATPase activity of SecA is regulated by acidic phospholipids, SecY, and the leader and mature domains of precursor proteins. Cell 60, 271-280.(doi:10.1016/0092-8674(90)90742-W)
    • (1990) Cell , vol.60 , pp. 271-280
    • Lill, R.1    Dowhan, W.2    Wickner, W.3
  • 78
    • 0026344236 scopus 로고
    • SecA protein needs both acidic phospholipids and SecY/E protein for functional high-affinity binding to the Escherichia coli plasma membrane
    • Hendrick, J. P. & Wickner, W. 1991 SecA protein needs both acidic phospholipids and SecY/E protein for functional high-affinity binding to the Escherichia coli plasma membrane. J. Biol. Chem. 266, 24596-24600.
    • (1991) J. Biol. Chem , vol.266 , pp. 24596-24600
    • Hendrick, J.P.1    Wickner, W.2
  • 79
    • 36048929458 scopus 로고    scopus 로고
    • A large conformational change couples the ATP binding site of SecA to the SecY protein channel
    • doi:10.1016/j.jmb.2007.09.086
    • Robson, A., Booth, A. E., Gold, V. A., Clarke, A. R. & Collinson, I. 2007 A large conformational change couples the ATP binding site of SecA to the SecY protein channel. J. Mol. Biol. 374, 965-976.(doi:10.1016/j.jmb.2007.09.086)
    • (2007) J. Mol. Biol , vol.374 , pp. 965-976
    • Robson, A.1    Booth, A.E.2    Gold, V.A.3    Clarke, A.R.4    Collinson, I.5
  • 80
    • 3343011973 scopus 로고    scopus 로고
    • A large conformational change of the translocation ATPase SecA
    • doi:10.1073/pnas.0401742101
    • Osborne, A. R., Clemons Jr, W. M. & Rapoport, T. A. 2004 A large conformational change of the translocation ATPase SecA. Proc. Natl Acad. Sci. USA 101, 10937-10942.(doi:10.1073/pnas.0401742101)
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 10937-10942
    • Osborne, A.R.1    Clemons, W.M.2    Rapoport, T.A.3
  • 81
    • 70449534599 scopus 로고    scopus 로고
    • Conformational flexibility and peptide interaction of the translocation ATPase SecA
    • doi:10.1016/j.jmb.2009.10.024
    • Zimmer, J. & Rapoport, T. A. 2009 Conformational flexibility and peptide interaction of the translocation ATPase SecA. J. Mol. Biol. 394, 606-612.(doi:10.1016/j.jmb.2009.10.024)
    • (2009) J. Mol. Biol , vol.394 , pp. 606-612
    • Zimmer, J.1    Rapoport, T.A.2
  • 82
    • 36049046667 scopus 로고    scopus 로고
    • Structural basis for signalsequence recognition by the translocase motor SecA as determined by NMR
    • doi:10.1016/j.cell.2007.09.039
    • Gelis, I., Bonvin, A. M., Keramisanou, D., Koukaki, M., Gouridis, G., Karamanou, S., Economou, A. & Kalodimos, C. G. 2007 Structural basis for signalsequence recognition by the translocase motor SecA as determined by NMR. Cell 131, 756-769.(doi:10.1016/j.cell.2007.09.039)
    • (2007) Cell , vol.131 , pp. 756-769
    • Gelis, I.1    Bonvin, A.M.2    Keramisanou, D.3    Koukaki, M.4    Gouridis, G.5    Karamanou, S.6    Economou, A.7    Kalodimos, C.G.8
  • 83
    • 33845667561 scopus 로고    scopus 로고
    • Selective photoaffinity labeling identifies the signal peptide binding domain on SecA
    • doi:10.1016/j.jmb.2006.10.027
    • Musial-Siwek, M., Rusch, S. L. & Kendall, D. A. 2007 Selective photoaffinity labeling identifies the signal peptide binding domain on SecA. J. Mol. Biol. 365, 637-648.(doi:10.1016/j.jmb.2006.10.027)
    • (2007) J. Mol. Biol , vol.365 , pp. 637-648
    • Musial-Siwek, M.1    Rusch, S.L.2    Kendall, D.A.3
  • 85
    • 0030703175 scopus 로고    scopus 로고
    • The molecular chaperone SecB is released from the carboxyterminus of SecA during initiation of precursor protein translocation
    • doi:10.1093/emboj/16.20.6105
    • Fekkes, P., van der Does, C. & Driessen, A. J. 1997 The molecular chaperone SecB is released from the carboxyterminus of SecA during initiation of precursor protein translocation. EMBO J. 16, 6105-6113.(doi:10.1093/emboj/16.20.6105)
    • (1997) EMBO J , vol.16 , pp. 6105-6113
    • Fekkes, P.1    van der Does, C.2    Driessen, A.J.3
  • 86
    • 0033586722 scopus 로고    scopus 로고
    • Zinc stabilizes the SecB binding site of SecA
    • doi:10.1021/bi982818r
    • Fekkes, P., de Wit, J. G., Boorsma, A., Friesen, R. H. & Driessen, A. J. 1999 Zinc stabilizes the SecB binding site of SecA. Biochemistry 38, 5111-5116.(doi:10.1021/bi982818r)
    • (1999) Biochemistry , vol.38 , pp. 5111-5116
    • Fekkes, P.1    de Wit, J.G.2    Boorsma, A.3    Friesen, R.H.4    Driessen, A.J.5
  • 87
    • 0242407175 scopus 로고    scopus 로고
    • Structural determinants of SecB recognition by SecA in bacterial protein translocation
    • doi:10.1038/nsb980
    • Zhou, J. & Xu, Z. 2003 Structural determinants of SecB recognition by SecA in bacterial protein translocation. Nat. Struct. Biol. 10, 942-947.(doi:10.1038/nsb980)
    • (2003) Nat. Struct. Biol , vol.10 , pp. 942-947
    • Zhou, J.1    Xu, Z.2
  • 88
    • 0028940082 scopus 로고
    • The C terminus of SecA is involved in both lipid binding and SecB binding
    • doi:10.1074/jbc.270.14.7902
    • Breukink, E., Nouwen, N., van Raalte, A., Mizushima, S., Tommassen, J. & de Kruijff, B. 1995 The C terminus of SecA is involved in both lipid binding and SecB binding. J. Biol. Chem. 270, 7902-7907.(doi:10.1074/jbc.270.14.7902)
    • (1995) J. Biol. Chem , vol.270 , pp. 7902-7907
    • Breukink, E.1    Nouwen, N.2    van Raalte, A.3    Mizushima, S.4    Tommassen, J.5    de Kruijff, B.6
  • 89
    • 0033428711 scopus 로고    scopus 로고
    • A molecular switch in SecA protein couples ATP hydrolysis to protein translocation
    • doi:10.1046/j.1365-2958.1999.01686.x
    • Karamanou, S., Vrontou, E., Sianidis, G., Baud, C., Roos, T., Kuhn, A., Politou, A. S. & Economou, A. 1999 A molecular switch in SecA protein couples ATP hydrolysis to protein translocation. Mol. Microbiol. 34, 1133-1145.(doi:10.1046/j.1365-2958.1999.01686.x)
    • (1999) Mol. Microbiol , vol.34 , pp. 1133-1145
    • Karamanou, S.1    Vrontou, E.2    Sianidis, G.3    Baud, C.4    Roos, T.5    Kuhn, A.6    Politou, A.S.7    Economou, A.8
  • 90
    • 2942588637 scopus 로고    scopus 로고
    • Nucleotide exchange from the high-affinity ATPbinding site in SecA is the rate-limiting step in the ATPase cycle of the soluble enzyme and occurs through a specialized conformational state
    • doi:10.1021/bi0357208
    • Fak, J. J., Itkin, A., Ciobanu, D. D., Lin, E. C., Song, X. J., Chou, Y. T., Gierasch, L. M. & Hunt, J. F. 2004 Nucleotide exchange from the high-affinity ATPbinding site in SecA is the rate-limiting step in the ATPase cycle of the soluble enzyme and occurs through a specialized conformational state. Biochemistry 43, 7307-7327.(doi:10.1021/bi0357208)
    • (2004) Biochemistry , vol.43 , pp. 7307-7327
    • Fak, J.J.1    Itkin, A.2    Ciobanu, D.D.3    Lin, E.C.4    Song, X.J.5    Chou, Y.T.6    Gierasch, L.M.7    Hunt, J.F.8
  • 91
    • 0035282958 scopus 로고    scopus 로고
    • Cross-talk between catalytic and regulatory elements in a DEAD motor domain is essential for SecA function
    • doi:10.1093/emboj/20.5.961
    • Sianidis, G., Karamanou, S., Vrontou, E., Boulias, K., Repanas, K., Kyrpides, N., Politou, A. S. & Economou, A. 2001 Cross-talk between catalytic and regulatory elements in a DEAD motor domain is essential for SecA function. EMBO J. 20, 961-970.(doi:10.1093/emboj/20.5.961)
    • (2001) EMBO J , vol.20 , pp. 961-970
    • Sianidis, G.1    Karamanou, S.2    Vrontou, E.3    Boulias, K.4    Repanas, K.5    Kyrpides, N.6    Politou, A.S.7    Economou, A.8
  • 92
    • 0025959111 scopus 로고
    • SecA, an essential component of the secretory machinery of Escherichia coli, exists as homodimer
    • doi:10.1016/0006-291X(91)90507-4
    • Akita, M., Shinkai, A., Matsuyama, S. & Mizushima, S. 1991 SecA, an essential component of the secretory machinery of Escherichia coli, exists as homodimer. Biochem. Biophys. Res. Commun. 174, 211-216.(doi:10.1016/0006-291X(91)90507-4)
    • (1991) Biochem. Biophys. Res. Commun , vol.174 , pp. 211-216
    • Akita, M.1    Shinkai, A.2    Matsuyama, S.3    Mizushima, S.4
  • 93
    • 79952470913 scopus 로고    scopus 로고
    • Quaternary structure of SecA in solution and bound to SecYEG probed at the single molecule level
    • doi:10.1016/j.str.2010.12.016
    • Kusters, I., van den Bogaart, G., Kedrov, A., Krasnikov, V., Fulyani, F., Poolman, B. & Driessen, A. J. 2011 Quaternary structure of SecA in solution and bound to SecYEG probed at the single molecule level. Structure 19, 430-439.(doi:10.1016/j.str.2010.12.016)
    • (2011) Structure , vol.19 , pp. 430-439
    • Kusters, I.1    van den Bogaart, G.2    Kedrov, A.3    Krasnikov, V.4    Fulyani, F.5    Poolman, B.6    Driessen, A.J.7
  • 94
    • 0042736538 scopus 로고    scopus 로고
    • Nucleotide binding induces changes in the oligomeric state and conformation of Sec A in a lipid environment: A small-angle neutron-scattering study
    • doi:10.1016/S0022-2836(03)00840-4
    • Bu, Z., Wang, L. & Kendall, D. A. 2003 Nucleotide binding induces changes in the oligomeric state and conformation of Sec A in a lipid environment: a small-angle neutron-scattering study. J. Mol. Biol. 332, 23-30.(doi:10.1016/S0022-2836(03)00840-4)
    • (2003) J. Mol. Biol , vol.332 , pp. 23-30
    • Bu, Z.1    Wang, L.2    Kendall, D.A.3
  • 95
    • 0037423278 scopus 로고    scopus 로고
    • Phospholipid-induced monomerization and signal-peptide-induced oligomerization of SecA
    • doi:10.1074/jbc.M205992200
    • Benach, J. et al. 2003 Phospholipid-induced monomerization and signal-peptide-induced oligomerization of SecA. J. Biol. Chem. 278, 3628-3638.(doi:10.1074/jbc.M205992200)
    • (2003) J. Biol. Chem , vol.278 , pp. 3628-3638
    • Benach, J.1
  • 96
    • 0027769773 scopus 로고
    • SecA, the peripheral subunit of the Escherichia coli precursor protein translocase, is functional as a dimer
    • Driessen, A. J. 1993 SecA, the peripheral subunit of the Escherichia coli precursor protein translocase, is functional as a dimer. Biochemistry 32, 13190-13197.
    • (1993) Biochemistry , vol.32 , pp. 13190-13197
    • Driessen, A.J.1
  • 97
    • 0037144467 scopus 로고    scopus 로고
    • Nucleotide control of interdomain interactions in the conformational reaction cycle of SecA
    • doi:10.1126/science.1074424
    • Hunt, J. F., Weinkauf, S., Henry, L., Fak, J. J., McNicholas, P., Oliver, D. B. & Deisenhofer, J. 2002 Nucleotide control of interdomain interactions in the conformational reaction cycle of SecA. Science 297, 2018-2026.(doi:10.1126/science.1074424)
    • (2002) Science , vol.297 , pp. 2018-2026
    • Hunt, J.F.1    Weinkauf, S.2    Henry, L.3    Fak, J.J.4    McNicholas, P.5    Oliver, D.B.6    Deisenhofer, J.7
  • 100
    • 33750846046 scopus 로고    scopus 로고
    • Crystal structure of the translocation ATPase SecA from Thermus thermophilus reveals a parallel, head-to-head dimer
    • doi:10.1016/j.jmb.2006.09.061
    • Vassylyev, D. G., Mori, H., Vassylyeva, M. N., Tsukazaki, T., Kimura, Y., Tahirov, T. H. & Ito, K. 2006 Crystal structure of the translocation ATPase SecA from Thermus thermophilus reveals a parallel, head-to-head dimer. J. Mol. Biol. 364, 248-258.(doi:10.1016/j.jmb.2006.09.061)
    • (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
  • 101
    • 33750821188 scopus 로고    scopus 로고
    • A novel dimer interface and conformational changes revealed by an X-ray structure of B. subtilis SecA
    • doi:10.1016/j.jmb.2006.08.044
    • Zimmer, J., Li, W. & Rapoport, T. A. 2006 A novel dimer interface and conformational changes revealed by an X-ray structure of B. subtilis SecA. J. Mol. Biol. 364, 259-265.(doi:10.1016/j.jmb.2006.08.044)
    • (2006) J. Mol. Biol , vol.364 , pp. 259-265
    • Zimmer, J.1    Li, W.2    Rapoport, T.A.3
  • 102
    • 0036129188 scopus 로고    scopus 로고
    • Complex behavior in solution of homodimeric SecA
    • doi:10.1110/ps.4090102
    • Woodbury, R. L., Hardy, S. J. & Randall, L. L. 2002 Complex behavior in solution of homodimeric SecA. Protein Sci. 11, 875-882.(doi:10.1110/ps.4090102)
    • (2002) Protein Sci , vol.11 , pp. 875-882
    • Woodbury, R.L.1    Hardy, S.J.2    Randall, L.L.3
  • 104
    • 0042347712 scopus 로고    scopus 로고
    • Bacillus subtilis SecA ATPase exists as an antiparallel dimer in solution
    • doi:10.1021/bi0342057
    • Ding, H., Hunt, J. F., Mukerji, I. & Oliver, D. 2003 Bacillus subtilis SecA ATPase exists as an antiparallel dimer in solution. Biochemistry 42, 8729-8738.(doi:10.1021/bi0342057)
    • (2003) Biochemistry , vol.42 , pp. 8729-8738
    • Ding, H.1    Hunt, J.F.2    Mukerji, I.3    Oliver, D.4
  • 105
    • 34247214427 scopus 로고    scopus 로고
    • Nanodiscs unravel the interaction between the SecYEG channel and its cytosolic partner SecA
    • doi:10.1038/sj.emboj.7601661
    • Alami, M., Dalal, K., Lelj-Garolla, B., Sligar, S. G. & Duong, F. 2007 Nanodiscs unravel the interaction between the SecYEG channel and its cytosolic partner SecA. EMBO J. 26, 1995-2004.(doi:10.1038/sj.emboj.7601661)
    • (2007) EMBO J , vol.26 , pp. 1995-2004
    • Alami, M.1    Dalal, K.2    Lelj-Garolla, B.3    Sligar, S.G.4    Duong, F.5
  • 106
    • 0037009514 scopus 로고    scopus 로고
    • Dissociation of the dimeric SecA ATPase during protein translocation across the bacterial membrane
    • doi:10.1093/emboj/cdf471
    • Or, E., Navon, A. & Rapoport, T. 2002 Dissociation of the dimeric SecA ATPase during protein translocation across the bacterial membrane. EMBO J. 21, 4470-4479.(doi:10.1093/emboj/cdf471)
    • (2002) EMBO J , vol.21 , pp. 4470-4479
    • Or, E.1    Navon, A.2    Rapoport, T.3
  • 107
    • 0041736710 scopus 로고    scopus 로고
    • Binding, activation and dissociation of the dimeric SecA ATPase at the dimeric SecYEG translocase
    • doi:10.1093/emboj/cdg418
    • Duong, F. 2003 Binding, activation and dissociation of the dimeric SecA ATPase at the dimeric SecYEG translocase. EMBO J. 22, 4375-4384.(doi:10.1093/emboj/cdg418)
    • (2003) EMBO J , vol.22 , pp. 4375-4384
    • Duong, F.1
  • 108
    • 33644904085 scopus 로고    scopus 로고
    • SecA dimer crosslinked at its subunit interface is functional for protein translocation
    • doi:10.1128/JB.188.1.335-338.2006
    • Jilaveanu, L. B. & Oliver, D. 2006 SecA dimer crosslinked at its subunit interface is functional for protein translocation. J. Bacteriol. 188, 335-338.(doi:10.1128/JB.188.1.335-338.2006)
    • (2006) J. Bacteriol , vol.188 , pp. 335-338
    • Jilaveanu, L.B.1    Oliver, D.2
  • 109
    • 38949141646 scopus 로고    scopus 로고
    • Additional in vitro and in vivo evidence for SecA functioning as dimers in the membrane: Dissociation into monomers is not essential for protein translocation in Escherichia coli
    • doi:10.1128/JB.01633-07
    • Wang, H., Na, B., Yang, H. & Tai, P. C. 2008 Additional in vitro and in vivo evidence for SecA functioning as dimers in the membrane: dissociation into monomers is not essential for protein translocation in Escherichia coli. J. Bacteriol. 190, 1413-1418.(doi:10.1128/JB.01633-07)
    • (2008) J. Bacteriol , vol.190 , pp. 1413-1418
    • Wang, H.1    Na, B.2    Yang, H.3    Tai, P.C.4
  • 110
    • 0023142279 scopus 로고
    • SecD, a new gene involved in protein export in Escherichia coli
    • Gardel, C., Benson, S., Hunt, J., Michaelis, S. & Beckwith, J. 1987 SecD, a new gene involved in protein export in Escherichia coli. J. Bacteriol. 169, 1286-1290.
    • (1987) J. Bacteriol , vol.169 , pp. 1286-1290
    • Gardel, C.1    Benson, S.2    Hunt, J.3    Michaelis, S.4    Beckwith, J.5
  • 111
    • 0025045470 scopus 로고
    • The secD locus of E. Coli Codes For Two Membrane Proteins Required For Protein Export
    • Gardel, C., Johnson, K., Jacq, A. & Beckwith, J. 1990 The secD locus of E. coli codes for two membrane proteins required for protein export. EMBO J. 9, 3209-3216.
    • (1990) EMBO J , vol.9 , pp. 3209-3216
    • Gardel, C.1    Johnson, K.2    Jacq, A.3    Beckwith, J.4
  • 112
    • 0027458691 scopus 로고
    • SecD is involved in the release of translocated secretory proteins from the cytoplasmic membrane of Escherichia coli
    • Matsuyama, S., Fujita, Y. & Mizushima, S. 1993 SecD is involved in the release of translocated secretory proteins from the cytoplasmic membrane of Escherichia coli. EMBO J. 12, 265-270.
    • (1993) EMBO J , vol.12 , pp. 265-270
    • Matsuyama, S.1    Fujita, Y.2    Mizushima, S.3
  • 113
    • 0026769684 scopus 로고
    • Overproduction, purification and characterization of SecD and SecF, integral membrane components of the protein translocation machinery of Escherichia coli
    • doi:10.1016/0167-4838(92)90130-6
    • Matsuyama, S., Fujita, Y., Sagara, K. & Mizushima, S. 1992 Overproduction, purification and characterization of SecD and SecF, integral membrane components of the protein translocation machinery of Escherichia coli. Biochim. Biophys. Acta 1122, 77-84.(doi:10.1016/0167-4838(92)90130-6)
    • (1992) Biochim. Biophys. Acta , vol.1122 , pp. 77-84
    • Matsuyama, S.1    Fujita, Y.2    Sagara, K.3    Mizushima, S.4
  • 114
    • 0028009577 scopus 로고
    • SecD and SecF facilitate protein export in Escherichia coli
    • Pogliano, J. A. & Beckwith, J. 1994 SecD and SecF facilitate protein export in Escherichia coli. EMBO J. 13, 554-561.
    • (1994) EMBO J , vol.13 , pp. 554-561
    • Pogliano, J.A.1    Beckwith, J.2
  • 115
    • 0027956170 scopus 로고
    • SecA protein is exposed to the periplasmic surface of the E. coli inner membrane in its active state
    • doi:10.1016/S0092-8674(94)90602-5
    • Kim, Y. J., Rajapandi, T. & Oliver, D. 1994 SecA protein is exposed to the periplasmic surface of the E. coli inner membrane in its active state. Cell 78, 845-853.(doi:10.1016/S0092-8674(94)90602-5)
    • (1994) Cell , vol.78 , pp. 845-853
    • Kim, Y.J.1    Rajapandi, T.2    Oliver, D.3
  • 116
    • 0029561762 scopus 로고
    • SecA membrane cycling at SecYEG is driven by distinct ATP binding and hydrolysis events and is regulated by SecD and SecF
    • doi:10.1016/0092-8674(95)90143-4
    • Economou, A., Pogliano, J. A., Beckwith, J., Oliver, D. B. & Wickner, W. 1995 SecA membrane cycling at SecYEG is driven by distinct ATP binding and hydrolysis events and is regulated by SecD and SecF. Cell 83, 1171-1181.(doi:10.1016/0092-8674(95)90143-4)
    • (1995) Cell , vol.83 , pp. 1171-1181
    • Economou, A.1    Pogliano, J.A.2    Beckwith, J.3    Oliver, D.B.4    Wickner, W.5
  • 117
    • 0030922143 scopus 로고    scopus 로고
    • The protease- protected 30 kDa domain of SecA is largely inaccessible to the membrane lipid phase
    • doi:10.1093/emboj/16.9.2188
    • Eichler, J., Brunner, J. & Wickner, W. 1997 The protease- protected 30 kDa domain of SecA is largely inaccessible to the membrane lipid phase. EMBO J. 16, 2188-2196.(doi:10.1093/emboj/16.9.2188)
    • (1997) EMBO J , vol.16 , pp. 2188-2196
    • Eichler, J.1    Brunner, J.2    Wickner, W.3
  • 118
    • 0030903689 scopus 로고    scopus 로고
    • Both an N-terminal 65-kDa domain and a C-terminal 30-kDa domain of SecA cycle into the membrane at SecYEG during translocation
    • doi:10.1073/pnas.94.11.5574
    • Eichler, J. & Wickner, W. 1997 Both an N-terminal 65-kDa domain and a C-terminal 30-kDa domain of SecA cycle into the membrane at SecYEG during translocation. Proc. Natl Acad. Sci. USA 94, 5574-5581.(doi:10.1073/pnas.94.11.5574)
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 5574-5581
    • Eichler, J.1    Wickner, W.2
  • 119
    • 0030745847 scopus 로고    scopus 로고
    • The SecDFyajC domain of preprotein translocase controls preprotein movement by regulating SecA membrane cycling
    • doi:10.1093/emboj/16.16.4871
    • Duong, F. & Wickner, W. 1997 The SecDFyajC domain of preprotein translocase controls preprotein movement by regulating SecA membrane cycling. EMBO J. 16, 4871-4879.(doi:10.1093/emboj/16.16.4871)
    • (1997) EMBO J , vol.16 , pp. 4871-4879
    • Duong, F.1    Wickner, W.2
  • 120
    • 23644461029 scopus 로고    scopus 로고
    • The large first periplasmic loop of SecD and SecF plays an important role in SecDF functioning
    • doi:10.1128/JB.187.16.5857-5860.2005
    • Nouwen, N., Piwowarek, M., Berrelkamp, G. & Driessen, A. J. 2005 The large first periplasmic loop of SecD and SecF plays an important role in SecDF functioning. J. Bacteriol. 187, 5857-5860.(doi:10.1128/JB.187.16.5857-5860.2005)
    • (2005) J. Bacteriol , vol.187 , pp. 5857-5860
    • Nouwen, N.1    Piwowarek, M.2    Berrelkamp, G.3    Driessen, A.J.4
  • 121
    • 79958281760 scopus 로고    scopus 로고
    • Structure and function of a membrane component SecDF that enhances protein export
    • doi:10.1038/nature09980
    • Tsukazaki, T. et al. 2011 Structure and function of a membrane component SecDF that enhances protein export. Nature 474, 235-238.(doi:10.1038/nature09980)
    • (2011) Nature , vol.474 , pp. 235-238
    • Tsukazaki, T.1
  • 123
    • 33748670458 scopus 로고    scopus 로고
    • Crystal structures of a multidrug transporter reveal a functionally rotating mechanism
    • doi:10.1038/nature05076
    • Murakami, S., Nakashima, R., Yamashita, E., Matsumoto, T. & Yamaguchi, A. 2006 Crystal structures of a multidrug transporter reveal a functionally rotating mechanism. Nature 443, 173-179.(doi:10.1038/nature05076)
    • (2006) Nature , vol.443 , pp. 173-179
    • Murakami, S.1    Nakashima, R.2    Yamashita, E.3    Matsumoto, T.4    Yamaguchi, A.5
  • 124
    • 0033170990 scopus 로고    scopus 로고
    • The RND permease superfamily: An ancient, ubiquitous and diverse family that includes human disease and development proteins
    • Tseng, T. T., Gratwick, K. S., Kollman, J., Park, D., Nies, D. H., Goffeau, A. & Saier Jr, M. H. 1999 The RND permease superfamily: an ancient, ubiquitous and diverse family that includes human disease and development proteins. J. Mol. Microbiol. Biotechnol. 1, 107-125.
    • (1999) J. Mol. Microbiol. Biotechnol , vol.1 , pp. 107-125
    • Tseng, T.T.1    Gratwick, K.S.2    Kollman, J.3    Park, D.4    Nies, D.H.5    Goffeau, A.6    Saier, M.H.7
  • 125
    • 0026073817 scopus 로고
    • Delta mu H{thorn} and ATP function at different steps of the catalytic cycle of preprotein translocase
    • doi:10.1016/0092-8674(91)90317-R
    • Schiebel, E., Driessen, A. J., Hartl, F. U. & Wickner, W. 1991 Delta mu H{thorn} and ATP function at different steps of the catalytic cycle of preprotein translocase. Cell 64, 927-939.(doi:10.1016/0092-8674(91)90317-R)
    • (1991) Cell , vol.64 , pp. 927-939
    • Schiebel, E.1    Driessen, A.J.2    Hartl, F.U.3    Wickner, W.4
  • 126
    • 0031435335 scopus 로고    scopus 로고
    • The catalytic cycle of the escherichia coli SecAATPase comprises two distinct preprotein translocation events
    • doi:10.1093/emboj/16.24.7297
    • van der Wolk, J. P., de Wit, J. G. & Driessen, A. J. 1997 The catalytic cycle of the escherichia coli SecAATPase comprises two distinct preprotein translocation events. EMBO J. 16, 7297-7304.(doi:10.1093/emboj/16.24.7297)
    • (1997) EMBO J , vol.16 , pp. 7297-7304
    • van der Wolk, J.P.1    de Wit, J.G.2    Driessen, A.J.3
  • 127
    • 0025968923 scopus 로고
    • Proton transfer is rate-limiting for translocation of precursor proteins by the Escherichia coli translocase
    • doi:10.1073/pnas.88.6.2471
    • Driessen, A. J. & Wickner, W. 1991 Proton transfer is rate-limiting for translocation of precursor proteins by the Escherichia coli translocase. Proc. Natl Acad. Sci. USA 88, 2471-2475.(doi:10.1073/pnas.88.6.2471)
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 2471-2475
    • Driessen, A.J.1    Wickner, W.2
  • 128
    • 0026540532 scopus 로고
    • Precursor protein translocation by the Escherichia coli translocase is directed by the protonmotive force
    • Driessen, A. J. 1992 Precursor protein translocation by the Escherichia coli translocase is directed by the protonmotive force. EMBO J. 11, 847-853.
    • (1992) EMBO J , vol.11 , pp. 847-853
    • Driessen, A.J.1
  • 129
    • 0028318253 scopus 로고
    • SecF stabilizes SecD and SecY, components of the protein translocation machinery of the Escherichia coli cytoplasmic membrane
    • Sagara, K., Matsuyama, S. & Mizushima, S. 1994 SecF stabilizes SecD and SecY, components of the protein translocation machinery of the Escherichia coli cytoplasmic membrane. J. Bacteriol. 176, 4111-4116.
    • (1994) J. Bacteriol , vol.176 , pp. 4111-4116
    • Sagara, K.1    Matsuyama, S.2    Mizushima, S.3
  • 130
    • 0036015653 scopus 로고    scopus 로고
    • SecDFyajC forms a heterotetrameric complex with YidC
    • doi:10.1046/j.1365-2958.2002.02972.x
    • Nouwen, N. & Driessen, A. J. 2002 SecDFyajC forms a heterotetrameric complex with YidC. Mol. Microbiol. 44, 1397-1405.(doi:10.1046/j.1365-2958.2002.02972.x)
    • (2002) Mol. Microbiol , vol.44 , pp. 1397-1405
    • Nouwen, N.1    Driessen, A.J.2
  • 131
    • 36749071555 scopus 로고    scopus 로고
    • Crystal structure of AcrB in complex with a single transmembrane subunit reveals another twist
    • doi:10.1016/j.str.2007.09.023
    • Tornroth-Horsefield, S., Gourdon, P., Horsefield, R., Brive, L., Yamamoto, N., Mori, H., Snijder, A. & Neutze, R. 2007 Crystal structure of AcrB in complex with a single transmembrane subunit reveals another twist. Structure 15, 1663-1673.(doi:10.1016/j.str.2007.09.023)
    • (2007) Structure , vol.15 , pp. 1663-1673
    • Tornroth-Horsefield, S.1    Gourdon, P.2    Horsefield, R.3    Brive, L.4    Yamamoto, N.5    Mori, H.6    Snijder, A.7    Neutze, R.8
  • 132
    • 79953320631 scopus 로고    scopus 로고
    • Expression, purification and characterization of the Escherichia coli integral membrane protein YajC
    • Fang, J. & Wei, Y. 2011 Expression, purification and characterization of the Escherichia coli integral membrane protein YajC. Protein Pept. Lett. 18, 601-608.
    • (2011) Protein Pept. Lett , vol.18 , pp. 601-608
    • Fang, J.1    Wei, Y.2
  • 133
    • 57649119791 scopus 로고    scopus 로고
    • Mechanisms of YidC-mediated insertion and assembly of multimeric membrane protein complexes
    • Kol, S., Nouwen, N. & Driessen, A. J. 2008 Mechanisms of YidC-mediated insertion and assembly of multimeric membrane protein complexes. J. Biol. Chem. 283, 31 269-31 273.
    • (2008) J. Biol. Chem. 283 , vol.283
    • Kol, S.1    Nouwen, N.2    Driessen, A.J.3
  • 134
    • 0028064967 scopus 로고
    • SecA promotes preprotein translocation by undergoing ATP-driven cycles of membrane insertion and deinsertion
    • doi:10.1016/S0092-8674(94)90582-7
    • Economou, A. & Wickner, W. 1994 SecA promotes preprotein translocation by undergoing ATP-driven cycles of membrane insertion and deinsertion. Cell 78, 835-843.(doi:10.1016/S0092-8674(94)90582-7)
    • (1994) Cell , vol.78 , pp. 835-843
    • Economou, A.1    Wickner, W.2
  • 135
    • 33947512486 scopus 로고    scopus 로고
    • In vivo membrane topology of Escherichia coli SecA ATPase reveals extensive periplasmic exposure of multiple functionally important domains clustering on one face of SecA
    • doi:10.1074/jbc.M610828200
    • Jilaveanu, L. B. & Oliver, D. B. 2007 In vivo membrane topology of Escherichia coli SecA ATPase reveals extensive periplasmic exposure of multiple functionally important domains clustering on one face of SecA. J. Biol. Chem. 282, 4661-4668.(doi:10.1074/jbc.M610828200)
    • (2007) J. Biol. Chem , vol.282 , pp. 4661-4668
    • Jilaveanu, L.B.1    Oliver, D.B.2
  • 136
    • 0029566085 scopus 로고
    • Stepwise movement of preproteins in the process of translocation across the cytoplasmic membrane of Escherichia coli
    • Uchida, K., Mori, H. & Mizushima, S. 1995 Stepwise movement of preproteins in the process of translocation across the cytoplasmic membrane of Escherichia coli. J. Biol. Chem. 270, 30862-30868.
    • (1995) J. Biol. Chem , vol.270 , pp. 30862-30868
    • Uchida, K.1    Mori, H.2    Mizushima, S.3
  • 137
    • 54049142467 scopus 로고    scopus 로고
    • A role for the two-helix finger of the SecA ATPase in protein translocation
    • doi:10.1038/nature07439
    • Erlandson, K. J., Miller, S. B., Nam, Y., Osborne, A. R., Zimmer, J. & Rapoport, T. A. 2008 A role for the two-helix finger of the SecA ATPase in protein translocation. Nature 455, 984-987.(doi:10.1038/nature07439)
    • (2008) Nature , vol.455 , pp. 984-987
    • Erlandson, K.J.1    Miller, S.B.2    Nam, Y.3    Osborne, A.R.4    Zimmer, J.5    Rapoport, T.A.6
  • 138
    • 60149105036 scopus 로고    scopus 로고
    • Charged amino acids in a preprotein inhibit SecAdependent protein translocation
    • doi:10.1016/j.jmb.2009.01.031
    • Nouwen, N., Berrelkamp, G. & Driessen, A. J. 2009 Charged amino acids in a preprotein inhibit SecAdependent protein translocation. J. Mol. Biol. 386, 1000-1010.(doi:10.1016/j.jmb.2009.01.031)
    • (2009) J. Mol. Biol , vol.386 , pp. 1000-1010
    • Nouwen, N.1    Berrelkamp, G.2    Driessen, A.J.3
  • 139
    • 0026576592 scopus 로고
    • What drives the translocation of proteins
    • doi:10.1073/pnas.89.9.3770
    • Simon, S. M., Peskin, C. S. & Oster, G. F. 1992 What drives the translocation of proteins? Proc. Natl Acad. Sci. USA 89, 3770-3774.(doi:10.1073/pnas.89.9.3770)
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 3770-3774
    • Simon, S.M.1    Peskin, C.S.2    Oster, G.F.3
  • 140
    • 79958272283 scopus 로고    scopus 로고
    • SecA, a remarkable nanomachine
    • doi:10.1007/s00018-011-0681-y
    • Kusters, I. & Driessen, A. J. 2011 SecA, a remarkable nanomachine. Cell. Mol. Life Sci. 68, 2053-2066.(doi:10.1007/s00018-011-0681-y)
    • (2011) Cell. Mol. Life Sci , vol.68 , pp. 2053-2066
    • Kusters, I.1    Driessen, A.J.2
  • 141
    • 63449140188 scopus 로고    scopus 로고
    • Maximal efficiency of coupling between ATP hydrolysis and translocation of polypeptides mediated by SecB requires two protomers of SecA
    • doi:10.1128/JB.01321-08
    • Mao, C., Hardy, S. J. & Randall, L. L. 2009 Maximal efficiency of coupling between ATP hydrolysis and translocation of polypeptides mediated by SecB requires two protomers of SecA. J. Bacteriol. 191, 978-984.(doi:10.1128/JB.01321-08)
    • (2009) J. Bacteriol , vol.191 , pp. 978-984
    • Mao, C.1    Hardy, S.J.2    Randall, L.L.3
  • 142
    • 1842559293 scopus 로고    scopus 로고
    • Sites of interaction between SecA and the chaperone SecB, two proteins involved in export
    • doi:10.1110/ps.03410104
    • Randall, L. L., Crane, J. M., Liu, G. & Hardy, S. J. 2004 Sites of interaction between SecA and the chaperone SecB, two proteins involved in export. Protein Sci. 13, 1124-1133.(doi:10.1110/ps.03410104)
    • (2004) Protein Sci , vol.13 , pp. 1124-1133
    • Randall, L.L.1    Crane, J.M.2    Liu, G.3    Hardy, S.J.4
  • 144
    • 0019464222 scopus 로고
    • The spontaneous insertion of proteins into and across membranes: The helical hairpin hypothesis
    • doi:10.1016/0092-8674(81)90136-7
    • Engelman, D. M. & Steitz, T. A. 1981 The spontaneous insertion of proteins into and across membranes: the helical hairpin hypothesis. Cell 23, 411-422.(doi:10.1016/0092-8674(81)90136-7)
    • (1981) Cell , vol.23 , pp. 411-422
    • Engelman, D.M.1    Steitz, T.A.2
  • 145
    • 0027393014 scopus 로고
    • The SecA and SecY subunits of translocase are the nearest neighbors of a translocating preprotein, shielding it from phospholipids
    • Joly, J. C. & Wickner, W. 1993 The SecA and SecY subunits of translocase are the nearest neighbors of a translocating preprotein, shielding it from phospholipids. EMBO J. 12, 255-263.
    • (1993) EMBO J , vol.12 , pp. 255-263
    • Joly, J.C.1    Wickner, W.2
  • 146
    • 1842690648 scopus 로고    scopus 로고
    • Binding of SecA to the SecYEG complex accelerates the rate of nucleotide exchange on SecA
    • Natale, P., Swaving, J., van der Does, C., de Keyzer, J. & Driessen, A. J. 2004 Binding of SecA to the SecYEG complex accelerates the rate of nucleotide exchange on SecA. J. Biol. Chem. 279, 13769-13777.
    • (2004) J. Biol. Chem , vol.279 , pp. 13769-13777
    • Natale, P.1    Swaving, J.2    van der Does, C.3    de Keyzer, J.4    Driessen, A.J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.