메뉴 건너뛰기
Journal of Bacteriology
Volumn 196, Issue 2, 2014, Pages 367-377
Identification of YidC residues that define interactions with the sec apparatus
Author keywords

[No Author keywords available]
Indexed keywords

MEMBRANE PROTEIN; SECY PROTEIN; UNCLASSIFIED DRUG; YIDC PROTEIN;
EID: 84890911196     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.01095-13     Document Type: Article
Times cited : (10)
References (54)
  • 2
    • 0025854858 scopus 로고
    • A protein-conducting channel in the endoplasmic reticulum
    • Simon SM, Blobel G. 1991. A protein-conducting channel in the endoplasmic reticulum. Cell 65:371-380. http://dx.doi.org/10.1016/0092-8674(91)90455-8.
    • (1991) Cell , vol.65 , pp. 371-380
    • Simon, S.M.1    Blobel, G.2
  • 3
    • 0027985063 scopus 로고
    • Secretory proteins move through the endoplasmic reticulum membrane via an aqueous, gated pore
    • Crowley KS, Liao S, Worrell VE, Reinhart GD, Johnson AE. 1994. Secretory proteins move through the endoplasmic reticulum membrane via an aqueous, gated pore. Cell 78:461-471. http://dx.doi.org/10.1016/0092-8674(94)90424-3.
    • (1994) Cell , vol.78 , pp. 461-471
    • Crowley, K.S.1    Liao, S.2    Worrell, V.E.3    Reinhart, G.D.4    Johnson, A.E.5
  • 4
    • 0029017127 scopus 로고
    • FtsH is required for proteolytic elimination of uncomplexed forms of SecY, an essential protein translocase subunit
    • 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. U. S. A. 92:4532-4536. http://dx.doi.org/10.1073/pnas.92.10.4532.
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 4532-4536
    • Kihara, A.1    Akiyama, Y.2    Ito, K.3
  • 5
    • 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. http://dx.doi.org/10.1074/jbc.271.33.19908.
    • (1996) J. Biol. Chem. , vol.271 , pp. 19908-19914
    • Pohlschroder, M.1    Murphy, C.2    Beckwith, J.3
  • 6
    • 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 KI, 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
  • 7
    • 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
  • 8
    • 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
  • 10
    • 23644461029 scopus 로고    scopus 로고
    • The large first periplasmic loop of SecD and SecF plays an important role in SecDF functioning
    • Nouwen N, Piwowarek M, Berrelkamp G, Driessen AJ. 2005. The large first periplasmic loop of SecD and SecF plays an important role in SecDF functioning. J. Bacteriol. 187:5857-5860. http://dx.doi.org/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
  • 12
    • 0031435335 scopus 로고    scopus 로고
    • The catalytic cycle of the Escherichia coli SecA ATPase comprises two distinct preprotein translocation events
    • van der Wolk JP, de Wit JG, Driessen AJ. 1997. The catalytic cycle of the Escherichia coli SecA ATPase comprises two distinct preprotein translocation events. EMBO J. 16:7297-7304. http://dx.doi.org/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
  • 13
    • 0026073817 scopus 로고
    • Delta mu H+ and ATP function at different steps of the catalytic cycle of preprotein translocase
    • Schiebel E, Driessen AJ, Hartl FU, Wickner W. 1991. Delta mu H+ and ATP function at different steps of the catalytic cycle of preprotein translocase. Cell 64:927-939. http://dx.doi.org/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
  • 14
    • 18844444516 scopus 로고    scopus 로고
    • OxaI/Alb3/YidC system for insertion of membrane proteins in mitochondria, chloroplasts and bacteria (review)
    • Yi L, Dalbey RE. 2005. OxaI/Alb3/YidC system for insertion of membrane proteins in mitochondria, chloroplasts and bacteria (review). Mol. Membr. Biol. 22:101-111. http://dx.doi.org/10.1080/09687860500041718.
    • (2005) Mol. Membr. Biol. , vol.22 , pp. 101-111
    • Yi, L.1    Dalbey, R.E.2
  • 15
    • 39149133696 scopus 로고    scopus 로고
    • Inserting proteins into the bacterial cytoplasmic membrane using the Sec and YidC translocases
    • Xie K, Dalbey RE. 2008. Inserting proteins into the bacterial cytoplasmic membrane using the Sec and YidC translocases. Nat. Rev. Microbiol. 6:234-244. http://dx.doi.org/10.1038/nrmicro1845.
    • (2008) Nat. Rev. Microbiol. , vol.6 , pp. 234-244
    • Xie, K.1    Dalbey, R.E.2
  • 16
    • 57649119791 scopus 로고    scopus 로고
    • Mechanisms of YidC-mediated insertionandassembly of multimericmembraneprotein complexes
    • Kol S, Nouwen N, Driessen AJ. 2008. Mechanisms of YidC-mediated insertionandassembly of multimericmembraneprotein complexes. J. Biol.Chem. 283:31269-31273. http://dx.doi.org/10.1074/jbc.R800029200.
    • (2008) J. Biol.Chem. , vol.283 , pp. 31269-31273
    • Kol, S.1    Nouwen, N.2    Driessen, A.J.3
  • 17
    • 0035856567 scopus 로고    scopus 로고
    • Phylogenetic and structural analyses of the oxa1 family of protein translocases
    • Yen MR, Harley KT, Tseng YH, Saier MH, Jr. 2001. Phylogenetic and structural analyses of the oxa1 family of protein translocases. FEMS Microbiol. Lett. 204:223-231. http://dx.doi.org/10.1111/j.1574-6968.2001.tb10889.x.
    • (2001) FEMS Microbiol. Lett. , vol.204 , pp. 223-231
    • Yen, M.R.1    Harley, K.T.2    Tseng, Y.H.3    Saier, M.H.4
  • 20
    • 2142705713 scopus 로고    scopus 로고
    • F1F0 ATP synthase subunit c is a substrate of the novel YidC pathway for membrane protein biogenesis
    • van der Laan M, Bechtluft P, Kol S, Nouwen N, Driessen AJ. 2004. F1F0 ATP synthase subunit c is a substrate of the novel YidC pathway for membrane protein biogenesis. J. Cell Biol. 165:213-222. http://dx.doi.org/10.1083/jcb.200402100.
    • (2004) J. Cell Biol. , vol.165 , pp. 213-222
    • van der Laan, M.1    Bechtluft, P.2    Kol, S.3    Nouwen, N.4    Driessen, A.J.5
  • 21
    • 4544234959 scopus 로고    scopus 로고
    • Sec/SRP requirements and energetics of membrane insertion of subunits a, b, and c of the Escherichia coli F1F0 ATP synthase
    • Yi L, Celebi N, Chen M, Dalbey RE. 2004. Sec/SRP requirements and energetics of membrane insertion of subunits a, b, and c of the Escherichia coli F1F0 ATP synthase. J. Biol. Chem. 279:39260-39267. http://dx.doi.org/10.1074/jbc.M405490200.
    • (2004) J. Biol. Chem. , vol.279 , pp. 39260-39267
    • Yi, L.1    Celebi, N.2    Chen, M.3    Dalbey, R.E.4
  • 22
    • 33845761509 scopus 로고    scopus 로고
    • The mechanosensitive channel protein MscL is targeted by the SRP to the novel YidC membrane insertion pathway of Escherichia coli
    • Facey SJ, Neugebauer SA, Krauss S, Kuhn A. 2007. The mechanosensitive channel protein MscL is targeted by the SRP to the novel YidC membrane insertion pathway of Escherichia coli. J. Mol. Biol. 365:995-1004. http://dx.doi.org/10.1016/j.jmb.2006.10.083.
    • (2007) J. Mol. Biol. , vol.365 , pp. 995-1004
    • Facey, S.J.1    Neugebauer, S.A.2    Krauss, S.3    Kuhn, A.4
  • 23
    • 19744376674 scopus 로고    scopus 로고
    • Global topology analysis of the Escherichia coli inner membrane proteome
    • Daley DO, Rapp M, Granseth E, Melen K, Drew D, von Heijne G. 2005. Global topology analysis of the Escherichia coli inner membrane proteome. Science 308:1321-1323. http://dx.doi.org/10.1126/science.1109730.
    • (2005) Science , vol.308 , pp. 1321-1323
    • Daley, D.O.1    Rapp, M.2    Granseth, E.3    Melen, K.4    Drew, D.5    von Heijne, G.6
  • 24
    • 0031892162 scopus 로고    scopus 로고
    • How many membrane proteins are there?
    • Boyd D, Schierle C, Beckwith J. 1998. How many membrane proteins are there? Protein Sci. 7:201-205. http://dx.doi.org/10.1002/pro.5560070121.
    • (1998) Protein Sci , vol.7 , pp. 201-205
    • Boyd, D.1    Schierle, C.2    Beckwith, J.3
  • 25
    • 84855239343 scopus 로고    scopus 로고
    • Unbalanced charge distribution as a determinant for dependence of a subset of Escherichia coli membrane proteins on the membrane insertase YidC
    • Gray AN, Henderson-Frost JM, Boyd D, Shirafi S, Niki H, Goldberg MB. 2011. Unbalanced charge distribution as a determinant for dependence of a subset of Escherichia coli membrane proteins on the membrane insertase YidC. mBio 2:00238-00211. http://dx.doi.org/10.1128/mBio.00238-11.
    • (2011) mBio , vol.2 , pp. 00238-00211
    • Gray, A.N.1    Henderson-Frost, J.M.2    Boyd, D.3    Shirafi, S.4    Niki, H.5    Goldberg, M.B.6
  • 26
    • 77956555964 scopus 로고    scopus 로고
    • Differential effect of YidC depletion on the membrane proteome of Escherichia coli under aerobic and anaerobic growth conditions
    • Price CE, Otto A, Fusetti F, Becher D, Hecker M, Driessen AJ. 2010. Differential effect of YidC depletion on the membrane proteome of Escherichia coli under aerobic and anaerobic growth conditions. Proteomics 10:3235-3247. http://dx.doi.org/10.1002/pmic.201000284.
    • (2010) Proteomics , vol.10 , pp. 3235-3247
    • Price, C.E.1    Otto, A.2    Fusetti, F.3    Becher, D.4    Hecker, M.5    Driessen, A.J.6
  • 27
    • 0034859711 scopus 로고    scopus 로고
    • YidC, an assembly site for polytopic Escherichia coli membrane proteins located in immediate proximity to the SecYE translocon and lipids
    • Beck K, Eisner G, Trescher D, Dalbey RE, Brunner J, Muller M. 2001. YidC, an assembly site for polytopic Escherichia coli membrane proteins located in immediate proximity to the SecYE translocon and lipids. EMBO Rep. 2:709-714. http://dx.doi.org/10.1093/embo-reports/kve154.
    • (2001) EMBO Rep. , vol.2 , pp. 709-714
    • Beck, K.1    Eisner, G.2    Trescher, D.3    Dalbey, R.E.4    Brunner, J.5    Muller, M.6
  • 28
    • 0347157958 scopus 로고    scopus 로고
    • The Alb3/OxaI/YidC protein family: membrane-localized chaperones facilitating membrane protein insertion?
    • Kuhn A, Stuart R, Henry R, Dalbey RE. 2003. The Alb3/OxaI/YidC protein family: membrane-localized chaperones facilitating membrane protein insertion? Trends Cell Biol. 13:510-516. http://dx.doi.org/10.1016/j.tcb.2003.08.005.
    • (2003) Trends Cell Biol , vol.13 , pp. 510-516
    • Kuhn, A.1    Stuart, R.2    Henry, R.3    Dalbey, R.E.4
  • 29
    • 84878746549 scopus 로고    scopus 로고
    • YidC occupies the lateral gate of the SecYEG translocon and is sequentially displaced by a nascent membrane protein
    • Sachelaru I, Petriman NA, Kudva R, Kuhn P, Welte T, Knapp B, Drepper F, Warscheid B, Koch HG. 2013. YidC occupies the lateral gate of the SecYEG translocon and is sequentially displaced by a nascent membrane protein. J. Biol. Chem. 288:16295-16307. http://dx.doi.org/10.1074/jbc.M112.446583.
    • (2013) J. Biol. Chem. , vol.288 , pp. 16295-16307
    • Sachelaru, I.1    Petriman, N.A.2    Kudva, R.3    Kuhn, P.4    Welte, T.5    Knapp, B.6    Drepper, F.7    Warscheid, B.8    Koch, H.G.9
  • 30
    • 37349111755 scopus 로고    scopus 로고
    • Projection structure of yidC: a conserved mediator of membrane protein assembly
    • Lotz M, Haase W, Kuhlbrandt W, Collinson I. 2008. Projection structure of yidC: a conserved mediator of membrane protein assembly. J. Mol. Biol. 375:901-907. http://dx.doi.org/10.1016/j.jmb.2007.10.089.
    • (2008) J. Mol. Biol. , vol.375 , pp. 901-907
    • Lotz, M.1    Haase, W.2    Kuhlbrandt, W.3    Collinson, I.4
  • 31
    • 33750699295 scopus 로고    scopus 로고
    • Different regions of the nonconserved large periplasmic domain of Escherichia coli YidC are involved in the SecF interaction and membrane insertase activity
    • Xie K, Kiefer D, Nagler G, Dalbey RE, Kuhn A. 2006. Different regions of the nonconserved large periplasmic domain of Escherichia coli YidC are involved in the SecF interaction and membrane insertase activity. Biochemistry 45:13401-13408. http://dx.doi.org/10.1021/bi060826z.
    • (2006) Biochemistry , vol.45 , pp. 13401-13408
    • Xie, K.1    Kiefer, D.2    Nagler, G.3    Dalbey, R.E.4    Kuhn, A.5
  • 32
    • 0025675856 scopus 로고
    • High efficiency transformation of Escherichia coli with plasmids
    • Inoue H, Nojima H, Okayama H. 1990. High efficiency transformation of Escherichia coli with plasmids. Gene 96:23-28. http://dx.doi.org/10.1016/0378-1119(90)90336-P.
    • (1990) Gene , vol.96 , pp. 23-28
    • Inoue, H.1    Nojima, H.2    Okayama, H.3
  • 34
    • 0036015653 scopus 로고    scopus 로고
    • SecDFyajC forms a heterotetrameric complex with YidC
    • Nouwen N, Driessen AJ. 2002. SecDFyajC forms a heterotetrameric complex with YidC. Mol. Microbiol. 44:1397-1405. http://dx.doi.org/10.1046/j.1365-2958.2002.02972.x.
    • (2002) Mol. Microbiol. , vol.44 , pp. 1397-1405
    • Nouwen, N.1    Driessen, A.J.2
  • 35
    • 84869389750 scopus 로고    scopus 로고
    • The YidC/OxaI/Alb3 protein family: common principles and distinct features
    • Saller MJ, Wu ZC, de Keyzer J, Driessen AJ. 2012. The YidC/OxaI/Alb3 protein family: common principles and distinct features. Biol. Chem. 393:1279-1290. http://dx.doi.org/10.1515/hsz-2012-0199.
    • (2012) Biol. Chem. , vol.393 , pp. 1279-1290
    • Saller, M.J.1    Wu, Z.C.2    de Keyzer, J.3    Driessen, A.J.4
  • 36
    • 0027081499 scopus 로고
    • Structure and function of the spoIIIJ gene of Bacillus subtilis: a vegetatively expressed gene that is essential for sigma G activity at an intermediate stage of sporulation
    • Errington J, Appleby L, Daniel RA, Goodfellow H, Partridge SR, Yudkin MD. 1992. Structure and function of the spoIIIJ gene of Bacillus subtilis: a vegetatively expressed gene that is essential for sigma G activity at an intermediate stage of sporulation. J. Gen. Microbiol. 138:2609-2618. http://dx.doi.org/10.1099/00221287-138-12-2609.
    • (1992) J. Gen. Microbiol. , vol.138 , pp. 2609-2618
    • Errington, J.1    Appleby, L.2    Daniel, R.A.3    Goodfellow, H.4    Partridge, S.R.5    Yudkin, M.D.6
  • 37
    • 41549128515 scopus 로고    scopus 로고
    • Functional overlap but lack of complete cross-complementation of Streptococcus mutans and Escherichia coli YidC orthologs
    • Dong Y, Palmer SR, Hasona A, Nagamori S, Kaback HR, Dalbey RE, Brady LJ. 2008. Functional overlap but lack of complete cross-complementation of Streptococcus mutans and Escherichia coli YidC orthologs. J. Bacteriol. 190:2458-2469. http://dx.doi.org/10.1128/JB.01366-07.
    • (2008) J. Bacteriol. , vol.190 , pp. 2458-2469
    • Dong, Y.1    Palmer, S.R.2    Hasona, A.3    Nagamori, S.4    Kaback, H.R.5    Dalbey, R.E.6    Brady, L.J.7
  • 38
    • 79251472718 scopus 로고    scopus 로고
    • Lipoproteins of bacterial pathogens
    • Kovacs-Simon A, Titball RW, Michell SL. 2011. Lipoproteins of bacterial pathogens. Infect. Immun. 79:548-561. http://dx.doi.org/10.1128/IAI.00682-10.
    • (2011) Infect. Immun. , vol.79 , pp. 548-561
    • Kovacs-Simon, A.1    Titball, R.W.2    Michell, S.L.3
  • 40
    • 2442585126 scopus 로고    scopus 로고
    • Role of YidC in folding of polytopic membrane proteins
    • Nagamori S, Smirnova IN, Kaback HR. 2004. Role of YidC in folding of polytopic membrane proteins. J. Cell Biol. 165:53-62. http://dx.doi.org/10.1083/jcb.200402067.
    • (2004) J. Cell Biol. , vol.165 , pp. 53-62
    • Nagamori, S.1    Smirnova, I.N.2    Kaback, H.R.3
  • 41
    • 0028009577 scopus 로고
    • SecD and SecF facilitate protein export in Escherichia coli
    • Pogliano JA, 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
  • 42
    • 0020727607 scopus 로고
    • A temperature-sensitive mutant of E. coli exhibiting slow processing of exported proteins
    • Ito K, Wittekind M, Nomura M, Shiba K, Yura T, Miura A, Nashimoto H. 1983. A temperature-sensitive mutant of E. coli exhibiting slow processing of exported proteins. Cell 32:789-797. http://dx.doi.org/10.1016/0092-8674(83)90065-X.
    • (1983) Cell , vol.32 , pp. 789-797
    • Ito, K.1    Wittekind, M.2    Nomura, M.3    Shiba, K.4    Yura, T.5    Miura, A.6    Nashimoto, H.7
  • 43
    • 1542676909 scopus 로고    scopus 로고
    • Defining the regions of Escherichia coli YidC that contribute to activity
    • Jiang F, Chen M, Yi L, de Gier JW, Kuhn A, Dalbey RE. 2003. Defining the regions of Escherichia coli YidC that contribute to activity. J. Biol. Chem. 278:48965-48972. http://dx.doi.org/10.1074/jbc.M307362200.
    • (2003) J. Biol. Chem. , vol.278 , pp. 48965-48972
    • Jiang, F.1    Chen, M.2    Yi, L.3    de Gier, J.W.4    Kuhn, A.5    Dalbey, R.E.6
  • 44
    • 41949094573 scopus 로고    scopus 로고
    • Crystal structure of the major periplasmic domain of the bacterial membrane protein assembly facilitator YidC
    • Oliver DC, Paetzel M. 2008. Crystal structure of the major periplasmic domain of the bacterial membrane protein assembly facilitator YidC. J. Biol. Chem. 283:5208-5216. http://dx.doi.org/10.1074/jbc.M708936200.
    • (2008) J. Biol. Chem. , vol.283 , pp. 5208-5216
    • Oliver, D.C.1    Paetzel, M.2
  • 45
    • 37449024146 scopus 로고    scopus 로고
    • Isolation of cold-sensitive yidC mutants provides insights into the substrate profile of the YidC insertase and the importance of transmembrane 3 in YidC function
    • Yuan J, Phillips GJ, Dalbey RE. 2007. Isolation of cold-sensitive yidC mutants provides insights into the substrate profile of the YidC insertase and the importance of transmembrane 3 in YidC function. J. Bacteriol. 189:8961-8972. http://dx.doi.org/10.1128/JB.01365-07.
    • (2007) J. Bacteriol. , vol.189 , pp. 8961-8972
    • Yuan, J.1    Phillips, G.J.2    Dalbey, R.E.3
  • 47
    • 65249159700 scopus 로고    scopus 로고
    • Visualization of distinct entities of the SecYEG translocon during translocation and integration of bacterial proteins
    • Boy D, Koch HG. 2009. Visualization of distinct entities of the SecYEG translocon during translocation and integration of bacterial proteins. Mol. Biol. Cell 20:1804-1815. http://dx.doi.org/10.1091/mbc.E08-08-0886.
    • (2009) Mol. Biol. Cell , vol.20 , pp. 1804-1815
    • Boy, D.1    Koch, H.G.2
  • 48
    • 0034959718 scopus 로고    scopus 로고
    • Reconstitution of Sec-dependent membrane protein insertion: nascent FtsQ interacts with YidC in a SecYEG-dependent manner
    • van der Laan M, Houben EN, Nouwen N, Luirink J, Driessen AJ. 2001. Reconstitution of Sec-dependent membrane protein insertion: nascent FtsQ interacts with YidC in a SecYEG-dependent manner. EMBO Rep. 2:519-523. http://dx.doi.org/10.1093/embo-reports/kve106.
    • (2001) EMBO Rep. , vol.2 , pp. 519-523
    • van der Laan, M.1    Houben, E.N.2    Nouwen, N.3    Luirink, J.4    Driessen, A.J.5
  • 49
    • 84878768073 scopus 로고    scopus 로고
    • Dynamic structure of the translocon SecYEG in membrane: direct single molecule observations
    • Sanganna Gari RR, Frey NC, Mao C, Randall LL, King GM. 2013. Dynamic structure of the translocon SecYEG in membrane: direct single molecule observations. J. Biol. Chem. 288:16848-16854. http://dx.doi.org/10.1074/jbc.M113.471870.
    • (2013) J. Biol. Chem. , vol.288 , pp. 16848-16854
    • Sanganna Gari, R.R.1    Frey, N.C.2    Mao, C.3    Randall, L.L.4    King, G.M.5
  • 52
    • 4644356464 scopus 로고    scopus 로고
    • Membraneprotein integration and the role of the translocation channel
    • Rapoport TA, Goder V, Heinrich SU, Matlack KE. 2004. Membraneprotein integration and the role of the translocation channel. Trends Cell Biol. 14:568-575. http://dx.doi.org/10.1016/j.tcb.2004.09.002.
    • (2004) Trends Cell Biol. , vol.14 , pp. 568-575
    • Rapoport, T.A.1    Goder, V.2    Heinrich, S.U.3    Matlack, K.E.4
  • 53
    • 0032515148 scopus 로고    scopus 로고
    • Membrane topology of the 60-kDa Oxa1p homologue from Escherichia coli
    • Saaf A, Monne M, de Gier JW, von Heijne G. 1998. Membrane topology of the 60-kDa Oxa1p homologue from Escherichia coli. J. Biol. Chem. 273:30415-30418. http://dx.doi.org/10.1074/jbc.273.46.30415.
    • (1998) J. Biol. Chem. , vol.273 , pp. 30415-30418
    • Saaf, A.1    Monne, M.2    de Gier, J.W.3    von Heijne, G.4
  • 54
    • 0017129243 scopus 로고
    • Transposition and fusion of the lac genes to selected promoters in Escherichia coli using bacteriophage lambda and Mu
    • Casadaban MJ. 1976. Transposition and fusion of the lac genes to selected promoters in Escherichia coli using bacteriophage lambda and Mu. J. Mol. Biol. 104:541-555. http://dx.doi.org/10.1016/0022-2836(76)90119-4.
    • (1976) J. Mol. Biol. , vol.104 , pp. 541-555
    • Casadaban, M.J.1

* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.