메뉴 건너뛰기




Volumn 5, Issue MARCH2016, 2016, Pages

Multi-functional roles for the polypeptide transport associated domains of Toc75 in chloroplast protein import

Author keywords

[No Author keywords available]

Indexed keywords

CHLOROPLAST PROTEIN; POLYPEPTIDE; PROTEIN TRANSLOCASE; TOC75; UNCLASSIFIED DRUG; ARABIDOPSIS PROTEIN; MEMBRANE PROTEIN; PROTEIN PRECURSOR; TOC75 PROTEIN, ARABIDOPSIS;

EID: 84962286485     PISSN: None     EISSN: 2050084X     Source Type: Journal    
DOI: 10.7554/eLife.12631     Document Type: Article
Times cited : (41)

References (95)
  • 2
    • 79960974503 scopus 로고    scopus 로고
    • Structural basis of outer membrane protein biogenesis in bacteria
    • Albrecht R, Zeth K. 2011. Structural basis of outer membrane protein biogenesis in bacteria. The Journal of Biological Chemistry 286:27792–27803. doi: 10.1074/jbc.M111.238931
    • (2011) The Journal of Biological Chemistry , vol.286 , pp. 27792-27803
    • Albrecht, R.1    Zeth, K.2
  • 3
    • 79956017174 scopus 로고    scopus 로고
    • Dimerization of TOC receptor GTPases and its implementation for the control of protein import into chloroplasts
    • Aronsson H, Jarvis P. 2011. Dimerization of TOC receptor GTPases and its implementation for the control of protein import into chloroplasts. The Biochemical Journal 436:e1–e2. doi: 10.1042/BJ20110659
    • (2011) The Biochemical Journal , vol.436 , pp. e1-e2
    • Aronsson, H.1    Jarvis, P.2
  • 4
    • 84955147754 scopus 로고    scopus 로고
    • The structure of the b-barrel assembly machinery complex
    • Bakelar J, Buchanan SK, Noinaj N. 2016. The structure of the b-barrel assembly machinery complex. Science (New York, N.Y.) 351:180–186. doi: 10.1126/science.aad3460
    • (2016) Science (New York, N.Y.) , vol.351 , pp. 180-186
    • Bakelar, J.1    Buchanan, S.K.2    Noinaj, N.3
  • 6
    • 77956153485 scopus 로고    scopus 로고
    • Dissection of b-barrel outer membrane protein assembly pathways through characterizing BamA POTRA 1 mutants of Escherichia coli
    • Bennion D, Charlson ES, Coon E, Misra R. 2010. Dissection of b-barrel outer membrane protein assembly pathways through characterizing BamA POTRA 1 mutants of Escherichia coli. Molecular Microbiology 77:1153–1171. doi: 10.1111/j.1365-2958.2010.07280.x
    • (2010) Molecular Microbiology , vol.77 , pp. 1153-1171
    • Bennion, D.1    Charlson, E.S.2    Coon, E.3    Misra, R.4
  • 8
    • 0027690206 scopus 로고
    • Precursors of one integral and five lumenal thylakoid proteins are imported by isolated pea and barley thylakoids: Optimisation of in vitro assays
    • Brock IW, Hazell L, Michl D, Nielsen VS, Møller BL, Herrmann RG, Klösgen RB, Robinson C. 1993. Precursors of one integral and five lumenal thylakoid proteins are imported by isolated pea and barley thylakoids: optimisation of in vitro assays. Plant Molecular Biology 23:717–725. doi: 10.1007/BF00021527
    • (1993) Plant Molecular Biology , vol.23 , pp. 717-725
    • Brock, I.W.1    Hazell, L.2    Michl, D.3    Nielsen, V.S.4    Møller, B.L.5    Herrmann, R.G.6    Klösgen, R.B.7    Robinson, C.8
  • 10
    • 84869406456 scopus 로고    scopus 로고
    • The gateway to chloroplast: Re-defining the function of chloroplast receptor proteins
    • Chang WL, Soll J, Bölter B. 2012. The gateway to chloroplast: re-defining the function of chloroplast receptor proteins. Biological Chemistry 393:1263–1277. doi: 10.1515/hsz-2012-0235
    • (2012) Biological Chemistry , vol.393 , pp. 1263-1277
    • Chang, W.L.1    Soll, J.2    Bölter, B.3
  • 11
    • 0030965614 scopus 로고    scopus 로고
    • Insertion of the 34-kDa chloroplast protein import component, IAP34, into the chloroplast outer membrane is dependent on its intrinsic GTP-binding capacity
    • Chen D, Schnell DJ. 1997. Insertion of the 34-kDa chloroplast protein import component, IAP34, into the chloroplast outer membrane is dependent on its intrinsic GTP-binding capacity. The Journal of Biological Chemistry 272:6614–6620. doi: 10.1074/jbc.272.10.6614
    • (1997) The Journal of Biological Chemistry , vol.272 , pp. 6614-6620
    • Chen, D.1    Schnell, D.J.2
  • 12
    • 0036009919 scopus 로고    scopus 로고
    • In vivo analysis of the role of atTic20 in protein import into chloroplasts
    • Chen X, Smith MD, Fitzpatrick L, Schnell DJ. 2002. In vivo analysis of the role of atTic20 in protein import into chloroplasts. The Plant Cell 14:641–654. doi: 10.1105/tpc.010336
    • (2002) The Plant Cell , vol.14 , pp. 641-654
    • Chen, X.1    Smith, M.D.2    Fitzpatrick, L.3    Schnell, D.J.4
  • 13
    • 33845648130 scopus 로고    scopus 로고
    • Precursor binding to an 880-kDa Toc complex as an early step during active import of protein into chloroplasts
    • Chen KY, Li HM. 2007. Precursor binding to an 880-kDa Toc complex as an early step during active import of protein into chloroplasts. The Plant Journal: For Cell and Molecular Biology 49:149–158. doi: 10.1111/j.1365-313X.2006.02944.x
    • (2007) The Plant Journal: For Cell and Molecular Biology , vol.49 , pp. 149-158
    • Chen, K.Y.1    Li, H.M.2
  • 15
    • 0032447801 scopus 로고    scopus 로고
    • Floral dip: A simplified method for Agrobacterium-mediated transformation of Arabidopsis thaliana
    • Clough SJ, Bent AF. 1998. Floral dip: a simplified method for Agrobacterium-mediated transformation of Arabidopsis thaliana. The Plant Journal: For Cell and Molecular Biology 16:735–743. doi: 10.1046/j.1365-313x.1998.00343.x
    • (1998) The Plant Journal: For Cell and Molecular Biology , vol.16 , pp. 735-743
    • Clough, S.J.1    Bent, A.F.2
  • 16
    • 84908006665 scopus 로고    scopus 로고
    • Evolution and targeting of Omp85 homologs in the chloroplast outer envelope membrane
    • Day PM, Potter D, Inoue K. 2014. Evolution and targeting of Omp85 homologs in the chloroplast outer envelope membrane. Frontiers in Plant Science 5. doi: 10.3389/fpls.2014.00535
    • (2014) Frontiers in Plant Science , vol.5
    • Day, P.M.1    Potter, D.2    Inoue, K.3
  • 18
    • 0036305169 scopus 로고    scopus 로고
    • A Toc75-like protein import channel is abundant in chloroplasts
    • Eckart K, Eichacker L, Sohrt K, Schleiff E, Heins L, Soll J. 2002. A Toc75-like protein import channel is abundant in chloroplasts. EMBO Reports 3:557–562. doi: 10.1093/embo-reports/kvf110
    • (2002) EMBO Reports , vol.3 , pp. 557-562
    • Eckart, K.1    Eichacker, L.2    Sohrt, K.3    Schleiff, E.4    Heins, L.5    Soll, J.6
  • 19
    • 23344442676 scopus 로고    scopus 로고
    • The evolutionarily related beta-barrel polypeptide transporters from Pisum sativum and Nostoc PCC7120 contain two distinct functional domains
    • Ertel F, Mirus O, Bredemeier R, Moslavac S, Becker T, Schleiff E. 2005. The evolutionarily related beta-barrel polypeptide transporters from Pisum sativum and Nostoc PCC7120 contain two distinct functional domains. The Journal of Biological Chemistry 280:28281–28289. doi: 10.1074/jbc.M503035200
    • (2005) The Journal of Biological Chemistry , vol.280 , pp. 28281-28289
    • Ertel, F.1    Mirus, O.2    Bredemeier, R.3    Moslavac, S.4    Becker, T.5    Schleiff, E.6
  • 20
    • 0034895894 scopus 로고    scopus 로고
    • A method for isolating a high yield of Arabidopsis chloroplasts capable of efficient import of precursor proteins
    • Fitzpatrick LM, Keegstra K. 2001. A method for isolating a high yield of Arabidopsis chloroplasts capable of efficient import of precursor proteins. The Plant Journal: For Cell and Molecular Biology 27:59–65. doi: 10.1046/j.0960-7412.2001.01061.x
    • (2001) The Plant Journal: For Cell and Molecular Biology , vol.27 , pp. 59-65
    • Fitzpatrick, L.M.1    Keegstra, K.2
  • 21
    • 84871732373 scopus 로고    scopus 로고
    • Molecular chaperone involvement in chloroplast protein import
    • Flores-Pérez Ú, Jarvis P. 2013. Molecular chaperone involvement in chloroplast protein import. Biochimica Et Biophysica Acta 1833:332–340. doi: 10.1016/j.bbamcr.2012.03.019
    • (2013) Biochimica Et Biophysica Acta , vol.1833 , pp. 332-340
    • Flores-Pérez, Ú.1    Jarvis, P.2
  • 22
    • 57049171923 scopus 로고    scopus 로고
    • Crystal structure of YaeT: Conformational flexibility and substrate recognition
    • Gatzeva-Topalova PZ, Walton TA, Sousa MC. 2008. Crystal structure of YaeT: conformational flexibility and substrate recognition. Structure (London, England: 1993) 16:1873–1881. doi: 10.1016/j.str.2008.09.014
    • (2008) Structure (London, England: 1993) , vol.16 , pp. 1873-1881
    • Gatzeva-Topalova, P.Z.1    Walton, T.A.2    Sousa, M.C.3
  • 23
    • 34249810338 scopus 로고    scopus 로고
    • Effect of chromatin upon Agrobacterium T-DNA integration and transgene expression
    • Gelvin SB, Kim SI. 2007. Effect of chromatin upon Agrobacterium T-DNA integration and transgene expression. Biochimica Et Biophysica Acta 1769:410–421. doi: 10.1016/j.bbaexp.2007.04.005
    • (2007) Biochimica Et Biophysica Acta , vol.1769 , pp. 410-421
    • Gelvin, S.B.1    Kim, S.I.2
  • 24
    • 28244436432 scopus 로고    scopus 로고
    • Molecular architecture and function of the Omp85 family of proteins
    • Gentle IE, Burri L, Lithgow T. 2005. Molecular architecture and function of the Omp85 family of proteins. Molecular Microbiology 58:1216–1225. doi: 10.1111/j.1365-2958.2005.04906.x
    • (2005) Molecular Microbiology , vol.58 , pp. 1216-1225
    • Gentle, I.E.1    Burri, L.2    Lithgow, T.3
  • 26
    • 33846002342 scopus 로고    scopus 로고
    • The N-terminal domain of Tob55 has a receptor-like function in the biogenesis of mitochondrial beta-barrel proteins
    • Habib SJ, Waizenegger T, Niewienda A, Paschen SA, Neupert W, Rapaport D. 2007. The N-terminal domain of Tob55 has a receptor-like function in the biogenesis of mitochondrial beta-barrel proteins. The Journal of Cell Biology 176:77–88. doi: 10.1083/jcb.200602050
    • (2007) The Journal of Cell Biology , vol.176 , pp. 77-88
    • Habib, S.J.1    Waizenegger, T.2    Niewienda, A.3    Paschen, S.A.4    Neupert, W.5    Rapaport, D.6
  • 27
    • 0031464541 scopus 로고    scopus 로고
    • Reconstitution of a chloroplast protein import channel
    • Hinnah SC, Hill K, Wagner R, Schlicher T, Soll J. 1997. Reconstitution of a chloroplast protein import channel. The EMBO Journal 16:7351–7360. doi: 10.1093/emboj/16.24.7351
    • (1997) The EMBO Journal , vol.16 , pp. 7351-7360
    • Hinnah, S.C.1    Hill, K.2    Wagner, R.3    Schlicher, T.4    Soll, J.5
  • 28
    • 0035997027 scopus 로고    scopus 로고
    • The chloroplast protein import channel Toc75: Pore properties and interaction with transit peptides
    • Hinnah SC, Wagner R, Sveshnikova N, Harrer R, Soll J. 2002. The chloroplast protein import channel Toc75: pore properties and interaction with transit peptides. Biophysical Journal 83:899–911. doi: 10.1016/S0006-3495(02)75216-8
    • (2002) Biophysical Journal , vol.83 , pp. 899-911
    • Hinnah, S.C.1    Wagner, R.2    Sveshnikova, N.3    Harrer, R.4    Soll, J.5
  • 29
    • 77952479299 scopus 로고    scopus 로고
    • Two evolutionarily conserved essential beta-barrel proteins in the chloroplast outer envelope membrane
    • Hsu SC, Inoue K. 2009. Two evolutionarily conserved essential beta-barrel proteins in the chloroplast outer envelope membrane. Bioscience Trends 3:168–178.
    • (2009) Bioscience Trends , vol.3 , pp. 168-178
    • Hsu, S.C.1    Inoue, K.2
  • 30
    • 82755194799 scopus 로고    scopus 로고
    • OEP80, an essential protein paralogous to the chloroplast protein translocation channel Toc75, exists as a 70-kD protein in the Arabidopsis thaliana chloroplast outer envelope
    • Hsu SC, Nafati M, Inoue K. 2012. OEP80, an essential protein paralogous to the chloroplast protein translocation channel Toc75, exists as a 70-kD protein in the Arabidopsis thaliana chloroplast outer envelope. Plant Molecular Biology 78:147–158. doi: 10.1007/s11103-011-9853-2
    • (2012) Plant Molecular Biology , vol.78 , pp. 147-158
    • Hsu, S.C.1    Nafati, M.2    Inoue, K.3
  • 31
    • 80052411081 scopus 로고    scopus 로고
    • In vivo analyses of the roles of essential Omp85-related proteins in the chloroplast outer envelope membrane
    • Huang W, Ling Q, Bédard J, Lilley K, Jarvis P. 2011. In vivo analyses of the roles of essential Omp85-related proteins in the chloroplast outer envelope membrane. Plant Physiology 157:147–159. doi: 10.1104/pp.111.181891
    • (2011) Plant Physiology , vol.157 , pp. 147-159
    • Huang, W.1    Ling, Q.2    Bédard, J.3    Lilley, K.4    Jarvis, P.5
  • 32
    • 30944457193 scopus 로고    scopus 로고
    • Deletion of core components of the plastid protein import machinery causes differential arrest of embryo development in Arabidopsis thaliana
    • Hust B, Gutensohn M. 2006. Deletion of core components of the plastid protein import machinery causes differential arrest of embryo development in Arabidopsis thaliana. Plant Biology (Stuttgart, Germany) 8:18–30. doi: 10.1055/s-2005-873044
    • (2006) Plant Biology (Stuttgart, Germany) , vol.8 , pp. 18-30
    • Hust, B.1    Gutensohn, M.2
  • 33
    • 30944465751 scopus 로고    scopus 로고
    • Arabidopsis tic110 is essential for the assembly and function of the protein import machinery of plastids
    • Inaba T, Alvarez-Huerta M, Li M, Bauer J, Ewers C, Kessler F, Schnell DJ. 2005. Arabidopsis tic110 is essential for the assembly and function of the protein import machinery of plastids. The Plant Cell 17:1482–1496. doi: 10.1105/tpc.105.030700
    • (2005) The Plant Cell , vol.17 , pp. 1482-1496
    • Inaba, T.1    Alvarez-Huerta, M.2    Li, M.3    Bauer, J.4    Ewers, C.5    Kessler, F.6    Schnell, D.J.7
  • 34
    • 46249121083 scopus 로고    scopus 로고
    • Protein trafficking to plastids: One theme, many variations
    • Inaba T, Schnell DJ. 2008. Protein trafficking to plastids: one theme, many variations. The Biochemical Journal 413:15–28. doi: 10.1042/BJ20080490
    • (2008) The Biochemical Journal , vol.413 , pp. 15-28
    • Inaba, T.1    Schnell, D.J.2
  • 35
    • 0034827035 scopus 로고    scopus 로고
    • The N-terminal portion of the preToc75 transit peptide interacts with membrane lipids and inhibits binding and import of precursor proteins into isolated chloroplasts
    • Inoue K, Demel R, de Kruijff B, Keegstra K. 2001. The N-terminal portion of the preToc75 transit peptide interacts with membrane lipids and inhibits binding and import of precursor proteins into isolated chloroplasts. European Journal of Biochemistry / FEBS 268:4036–4043. doi: 10.1046/j.1432-1327.2001.02316.x
    • (2001) European Journal of Biochemistry / FEBS , vol.268 , pp. 4036-4043
    • Inoue, K.1    Demel, R.2    De Kruijff, B.3    Keegstra, K.4
  • 36
    • 0038129640 scopus 로고    scopus 로고
    • A polyglycine stretch is necessary for proper targeting of the protein translocation channel precursor to the outer envelope membrane of chloroplasts
    • Inoue K, Keegstra K. 2003. A polyglycine stretch is necessary for proper targeting of the protein translocation channel precursor to the outer envelope membrane of chloroplasts. The Plant Journal: For Cell and Molecular Biology 34:661–669. doi: 10.1046/j.1365-313X.2003.01755.x
    • (2003) The Plant Journal: For Cell and Molecular Biology , vol.34 , pp. 661-669
    • Inoue, K.1    Keegstra, K.2
  • 37
    • 3843058949 scopus 로고    scopus 로고
    • The chloroplastic protein translocation channel Toc75 and its paralog OEP80 represent two distinct protein families and are targeted to the chloroplastic outer envelope by different mechanisms
    • Inoue K, Potter D. 2004. The chloroplastic protein translocation channel Toc75 and its paralog OEP80 represent two distinct protein families and are targeted to the chloroplastic outer envelope by different mechanisms. The Plant Journal: For Cell and Molecular Biology 39:354–365. doi: 10.1111/j.1365-313X.2004.02135.x
    • (2004) The Plant Journal: For Cell and Molecular Biology , vol.39 , pp. 354-365
    • Inoue, K.1    Potter, D.2
  • 38
    • 84874281189 scopus 로고    scopus 로고
    • An essential role for chloroplast heat shock protein 90 (Hsp90C) in protein import into chloroplasts
    • Inoue H, Li M, Schnell DJ. 2013. An essential role for chloroplast heat shock protein 90 (Hsp90C) in protein import into chloroplasts. Proceedings of the National Academy of Sciences 110:3173–3178. doi: 10.1073/pnas.1219229110
    • (2013) Proceedings of the National Academy of Sciences , vol.110 , pp. 3173-3178
    • Inoue, H.1    Li, M.2    Schnell, D.J.3
  • 39
    • 3042724874 scopus 로고    scopus 로고
    • Members of the Toc159 import receptor family represent distinct pathways for protein targeting to plastids
    • Ivanova Y, Smith MD, Chen K, Schnell DJ. 2004. Members of the Toc159 import receptor family represent distinct pathways for protein targeting to plastids. Molecular Biology of the Cell 15:3379–3392. doi: 10.1091/mbc.E03-12-0923
    • (2004) Molecular Biology of the Cell , vol.15 , pp. 3379-3392
    • Ivanova, Y.1    Smith, M.D.2    Chen, K.3    Schnell, D.J.4
  • 40
    • 0035037171 scopus 로고    scopus 로고
    • Arabidopsis genes encoding components of the chloroplastic protein import apparatus
    • Jackson-Constan D, Keegstra K. 2001. Arabidopsis genes encoding components of the chloroplastic protein import apparatus. Plant Physiology 125:1567–1576. doi: 10.1104/pp.125.4.1567
    • (2001) Plant Physiology , vol.125 , pp. 1567-1576
    • Jackson-Constan, D.1    Keegstra, K.2
  • 42
    • 84877666412 scopus 로고    scopus 로고
    • Evolutionary, molecular and genetic analyses of Tic22 homologues in Arabidopsis thaliana chloroplasts
    • Kasmati AR, Töpel M, Khan NZ, Patel R, Ling Q, Karim S, Aronsson H, Jarvis P. 2013. Evolutionary, molecular and genetic analyses of Tic22 homologues in Arabidopsis thaliana chloroplasts. PloS One 8:e63863. doi: 10.1371/journal.pone.0063863
    • (2013) Plos One , vol.8
    • Kasmati, A.R.1    Töpel, M.2    Khan, N.Z.3    Patel, R.4    Ling, Q.5    Karim, S.6    Aronsson, H.7    Jarvis, P.8
  • 43
    • 0027984260 scopus 로고
    • Identification of two GTP-binding proteins in the chloroplast protein import machinery
    • Kessler F, Blobel G, Patel HA, Schnell DJ. 1994. Identification of two GTP-binding proteins in the chloroplast protein import machinery. Science (New York, N.Y.) 266:1035–1039. doi: 10.1126/science.7973656
    • (1994) Science (New York, N.Y.) , vol.266 , pp. 1035-1039
    • Kessler, F.1    Blobel, G.2    Patel, H.A.3    Schnell, D.J.4
  • 44
    • 3042799389 scopus 로고    scopus 로고
    • Chloroplast protein import: Solve the GTPase riddle for entry
    • Kessler F, Schnell DJ. 2004. Chloroplast protein import: solve the GTPase riddle for entry. Trends in Cell Biology 14:334–338. doi: 10.1016/j.tcb.2004.05.004
    • (2004) Trends in Cell Biology , vol.14 , pp. 334-338
    • Kessler, F.1    Schnell, D.J.2
  • 45
    • 67949123338 scopus 로고    scopus 로고
    • Chloroplast biogenesis: Diversity and regulation of the protein import apparatus
    • Kessler F, Schnell D. 2009. Chloroplast biogenesis: diversity and regulation of the protein import apparatus. Current Opinion in Cell Biology 21:494–500. doi: 10.1016/j.ceb.2009.03.004
    • (2009) Current Opinion in Cell Biology , vol.21 , pp. 494-500
    • Kessler, F.1    Schnell, D.2
  • 46
    • 33645717179 scopus 로고    scopus 로고
    • Characterization of the preprotein translocon at the outer envelope membrane of chloroplasts by blue native PAGE
    • Kikuchi S, Hirohashi T, Nakai M. 2006. Characterization of the preprotein translocon at the outer envelope membrane of chloroplasts by blue native PAGE. Plant & Cell Physiology 47:363–371. doi: 10.1093/pcp/pcj002
    • (2006) Plant & Cell Physiology , vol.47 , pp. 363-371
    • Kikuchi, S.1    Hirohashi, T.2    Nakai, M.3
  • 47
    • 34548139422 scopus 로고    scopus 로고
    • Structure and function of an essential component of the outer membrane protein assembly machine
    • Kim S, Malinverni JC, Sliz P, Silhavy TJ, Harrison SC, Kahne D. 2007. Structure and function of an essential component of the outer membrane protein assembly machine. Science (New York, N.Y.) 317:961–964. doi: 10.1126/science.1143993
    • (2007) Science (New York, N.Y.) , vol.317 , pp. 961-964
    • Kim, S.1    Malinverni, J.C.2    Sliz, P.3    Silhavy, T.J.4    Harrison, S.C.5    Kahne, D.6
  • 48
    • 79951772443 scopus 로고    scopus 로고
    • Crystal structure of Escherichia coli BamB, a lipoprotein component of the b-barrel assembly machinery complex
    • Kim KH, Paetzel M. 2011. Crystal structure of Escherichia coli BamB, a lipoprotein component of the b-barrel assembly machinery complex. Journal of Molecular Biology 406:667–678. doi: 10.1016/j.jmb.2010.12.020
    • (2011) Journal of Molecular Biology , vol.406 , pp. 667-678
    • Kim, K.H.1    Paetzel, M.2
  • 49
    • 43449107064 scopus 로고    scopus 로고
    • Fold and function of polypeptide transport-associated domains responsible for delivering unfolded proteins to membranes
    • Knowles TJ, Jeeves M, Bobat S, Dancea F, McClelland D, Palmer T, Overduin M, Henderson IR. 2008. Fold and function of polypeptide transport-associated domains responsible for delivering unfolded proteins to membranes. Molecular Microbiology 68:1216–1227. doi: 10.1111/j.1365-2958.2008.06225.x
    • (2008) Molecular Microbiology , vol.68 , pp. 1216-1227
    • Knowles, T.J.1    Jeeves, M.2    Bobat, S.3    Dancea, F.4    McClelland, D.5    Palmer, T.6    Overduin, M.7    Henderson, I.R.8
  • 51
    • 0032539010 scopus 로고    scopus 로고
    • Tic20 and Tic22 are new components of the protein import apparatus at the chloroplast inner envelope membrane
    • Kouranov A, Chen X, Fuks B, Schnell DJ. 1998. Tic20 and Tic22 are new components of the protein import apparatus at the chloroplast inner envelope membrane. The Journal of Cell Biology 143:991–1002. doi: 10.1083/jcb.143.4.991
    • (1998) The Journal of Cell Biology , vol.143 , pp. 991-1002
    • Kouranov, A.1    Chen, X.2    Fuks, B.3    Schnell, D.J.4
  • 53
    • 84901059874 scopus 로고    scopus 로고
    • Specific targeting of proteins to outer envelope membranes of endosymbiotic organelles, chloroplasts, and mitochondria
    • Lee J, Kim DH, Hwang I. 2014. Specific targeting of proteins to outer envelope membranes of endosymbiotic organelles, chloroplasts, and mitochondria. Frontiers in Plant Science 5. doi: 10.3389/fpls.2014.00173
    • (2014) Frontiers in Plant Science , vol.5
    • Lee, J.1    Kim, D.H.2    Hwang, I.3
  • 54
    • 33750323349 scopus 로고    scopus 로고
    • Reconstitution of protein targeting to the inner envelope membrane of chloroplasts
    • Li M, Schnell DJ. 2006. Reconstitution of protein targeting to the inner envelope membrane of chloroplasts. The Journal of Cell Biology 175:249–259. doi: 10.1083/jcb.200605162
    • (2006) The Journal of Cell Biology , vol.175 , pp. 249-259
    • Li, M.1    Schnell, D.J.2
  • 55
    • 84880789245 scopus 로고    scopus 로고
    • Transit peptide design and plastid import regulation
    • Li HM, Teng YS. 2013. Transit peptide design and plastid import regulation. Trends in Plant Science 18:360–366. doi: 10.1016/j.tplants.2013.04.003
    • (2013) Trends in Plant Science , vol.18 , pp. 360-366
    • Li, H.M.1    Teng, Y.S.2
  • 56
    • 84931561206 scopus 로고    scopus 로고
    • Functions of plastid protein import and the ubiquitin-proteasome system in plastid development
    • Ling Q, Jarvis P. 2015. Functions of plastid protein import and the ubiquitin-proteasome system in plastid development. Biochimica Et Biophysica Acta 1847:939–948. doi: 10.1016/j.bbabio.2015.02.017
    • (2015) Biochimica Et Biophysica Acta , vol.1847 , pp. 939-948
    • Ling, Q.1    Jarvis, P.2
  • 57
    • 0029894578 scopus 로고    scopus 로고
    • Two components of the chloroplast protein import apparatus, IAP86 and IAP75, interact with the transit sequence during the recognition and translocation of precursor proteins at the outer envelope
    • Ma Y, Kouranov A, LaSala SE, Schnell DJ. 1996. Two components of the chloroplast protein import apparatus, IAP86 and IAP75, interact with the transit sequence during the recognition and translocation of precursor proteins at the outer envelope. The Journal of Cell Biology 134:315–327. doi: 10.1083/jcb.134.2.315
    • (1996) The Journal of Cell Biology , vol.134 , pp. 315-327
    • Ma, Y.1    Kouranov, A.2    Lasala, S.E.3    Schnell, D.J.4
  • 58
    • 0033729426 scopus 로고    scopus 로고
    • Generation of deletion and point mutations with one primer in a single cloning step
    • Makarova O, Kamberov E, Margolis B. 2000. Generation of deletion and point mutations with one primer in a single cloning step. BioTechniques 29:970–972.
    • (2000) Biotechniques , vol.29 , pp. 970-972
    • Makarova, O.1    Kamberov, E.2    Margolis, B.3
  • 59
    • 33745202589 scopus 로고    scopus 로고
    • YfiO stabilizes the YaeT complex and is essential for outer membrane protein assembly in Escherichia coli
    • Malinverni JC, Werner J, Kim S, Sklar JG, Kahne D, Misra R, Silhavy TJ. 2006. YfiO stabilizes the YaeT complex and is essential for outer membrane protein assembly in Escherichia coli. Molecular Microbiology 61:151–164. doi: 10.1111/j.1365-2958.2006.05211.x
    • (2006) Molecular Microbiology , vol.61 , pp. 151-164
    • Malinverni, J.C.1    Werner, J.2    Kim, S.3    Sklar, J.G.4    Kahne, D.5    Misra, R.6    Silhavy, T.J.7
  • 60
    • 79952311132 scopus 로고    scopus 로고
    • The crystal structure of BamB suggests interactions with BamA and its role within the BAM complex
    • Noinaj N, Fairman JW, Buchanan SK. 2011. The crystal structure of BamB suggests interactions with BamA and its role within the BAM complex. Journal of Molecular Biology 407:248–260. doi: 10.1016/j.jmb.2011.01.042
    • (2011) Journal of Molecular Biology , vol.407 , pp. 248-260
    • Noinaj, N.1    Fairman, J.W.2    Buchanan, S.K.3
  • 62
    • 84924962448 scopus 로고    scopus 로고
    • The b-barrel membrane protein insertase machinery from Gram-negative bacteria
    • Noinaj N, Rollauer SE, Buchanan SK. 2015. The b-barrel membrane protein insertase machinery from Gram-negative bacteria. Current Opinion in Structural Biology 31:35–42. doi: 10.1016/j.sbi.2015.02.012
    • (2015) Current Opinion in Structural Biology , vol.31 , pp. 35-42
    • Noinaj, N.1    Rollauer, S.E.2    Buchanan, S.K.3
  • 63
    • 0026571378 scopus 로고
    • The binding of precursor proteins to chloroplasts requires nucleoside triphosphates in the intermembrane space
    • Olsen LJ, Keegstra K. 1992. The binding of precursor proteins to chloroplasts requires nucleoside triphosphates in the intermembrane space. The Journal of Biological Chemistry 267:433–439.
    • (1992) The Journal of Biological Chemistry , vol.267 , pp. 433-439
    • Olsen, L.J.1    Keegstra, K.2
  • 64
    • 84923074903 scopus 로고    scopus 로고
    • New insights into the mechanism of chloroplast protein import and its integration with protein quality control, organelle biogenesis and development
    • Paila YD, Richardson LG, Schnell DJ. 2015. New insights into the mechanism of chloroplast protein import and its integration with protein quality control, organelle biogenesis and development. Journal of Molecular Biology 427:1038–1060. doi: 10.1016/j.jmb.2014.08.016
    • (2015) Journal of Molecular Biology , vol.427 , pp. 1038-1060
    • Paila, Y.D.1    Richardson, L.G.2    Schnell, D.J.3
  • 66
    • 55549098175 scopus 로고    scopus 로고
    • The Omp85-related chloroplast outer envelope protein OEP80 is essential for viability in Arabidopsis
    • Patel R, Hsu SC, Bédard J, Inoue K, Jarvis P. 2008. The Omp85-related chloroplast outer envelope protein OEP80 is essential for viability in Arabidopsis. Plant Physiology 148:235–245. doi: 10.1104/pp.108.122754
    • (2008) Plant Physiology , vol.148 , pp. 235-245
    • Patel, R.1    Hsu, S.C.2    Bédard, J.3    Inoue, K.4    Jarvis, P.5
  • 67
    • 84979561575 scopus 로고    scopus 로고
    • Targeting and assembly of components of the TOC protein import complex at the chloroplast outer envelope membrane
    • Richardson LG, Paila YD, Siman SR, Chen Y, Smith MD, Schnell DJ. 2014. Targeting and assembly of components of the TOC protein import complex at the chloroplast outer envelope membrane. Frontiers in Plant Science 5. doi: 10.3389/fpls.2014.00269
    • (2014) Frontiers in Plant Science , vol.5
    • Richardson, L.G.1    Paila, Y.D.2    Siman, S.R.3    Chen, Y.4    Smith, M.D.5    Schnell, D.J.6
  • 68
    • 0642377467 scopus 로고    scopus 로고
    • POTRA: A conserved domain in the FtsQ family and a class of beta-barrel outer membrane proteins
    • Sánchez-Pulido L, Devos D, Genevrois S, Vicente M, Valencia A. 2003. POTRA: a conserved domain in the FtsQ family and a class of beta-barrel outer membrane proteins. Trends in Biochemical Sciences 28:523–526. doi: 10.1016/j.tibs.2003.08.003
    • (2003) Trends in Biochemical Sciences , vol.28 , pp. 523-526
    • Sánchez-Pulido, L.1    Devos, D.2    Genevrois, S.3    Vicente, M.4    Valencia, A.5
  • 70
    • 27844456862 scopus 로고    scopus 로고
    • Membrane protein insertion: Mixing eukaryotic and prokaryotic concepts
    • Schleiff E, Soll J. 2005. Membrane protein insertion: mixing eukaryotic and prokaryotic concepts. EMBO Reports 6:1023–1027. doi: 10.1038/sj.embor.7400563
    • (2005) EMBO Reports , vol.6 , pp. 1023-1027
    • Schleiff, E.1    Soll, J.2
  • 71
    • 78651374569 scopus 로고    scopus 로고
    • Omp85 in eukaryotic systems: One protein family with distinct functions
    • Schleiff E, Maier UG, Becker T. 2011. Omp85 in eukaryotic systems: one protein family with distinct functions. Biological Chemistry 392:21–27. doi: 10.1515/BC.2011.005
    • (2011) Biological Chemistry , vol.392 , pp. 21-27
    • Schleiff, E.1    Maier, U.G.2    Becker, T.3
  • 72
    • 44949231424 scopus 로고    scopus 로고
    • Analyzing real-time PCR data by the comparative C(T) method
    • Schmittgen TD, Livak KJ. 2008. Analyzing real-time PCR data by the comparative C(T) method. Nature Protocols 3:1101–1108. doi: 10.1038/nprot.2008.73
    • (2008) Nature Protocols , vol.3 , pp. 1101-1108
    • Schmittgen, T.D.1    Livak, K.J.2
  • 74
    • 79851508389 scopus 로고    scopus 로고
    • Protein import into chloroplasts–how chaperones feature into the game
    • Schwenkert S, Soll J, Bölter B. 2011. Protein import into chloroplasts–how chaperones feature into the game. Biochimica Et Biophysica Acta 1808:901–911. doi: 10.1016/j.bbamem.2010.07.021
    • (2011) Biochimica Et Biophysica Acta , vol.1808 , pp. 901-911
    • Schwenkert, S.1    Soll, J.2    Bölter, B.3
  • 75
    • 84871749722 scopus 로고    scopus 로고
    • The chloroplast protein import system: From algae to trees
    • Shi LX, Theg SM. 2013. The chloroplast protein import system: from algae to trees. Biochimica Et Biophysica Acta 1833:314–331. doi: 10.1016/j.bbamcr.2012.10.002
    • (2013) Biochimica Et Biophysica Acta , vol.1833 , pp. 314-331
    • Shi, L.X.1    Theg, S.M.2
  • 76
    • 60749118851 scopus 로고    scopus 로고
    • Suborganellar localization of plastidic type I signal peptidase 1 depends on chloroplast development
    • Shipman RL, Inoue K. 2009. Suborganellar localization of plastidic type I signal peptidase 1 depends on chloroplast development. FEBS Letters 583:938–942. doi: 10.1016/j.febslet.2009.02.016
    • (2009) FEBS Letters , vol.583 , pp. 938-942
    • Shipman, R.L.1    Inoue, K.2
  • 77
    • 77949516026 scopus 로고    scopus 로고
    • The significance of protein maturation by plastidic type I signal peptidase 1 for thylakoid development in Arabidopsis chloroplasts
    • Shipman-Roston RL, Ruppel NJ, Damoc C, Phinney BS, Inoue K. 2010. The significance of protein maturation by plastidic type I signal peptidase 1 for thylakoid development in Arabidopsis chloroplasts. Plant Physiology 152: 1297–1308. doi: 10.1104/pp.109.151977
    • (2010) Plant Physiology , vol.152 , pp. 1297-1308
    • Shipman-Roston, R.L.1    Ruppel, N.J.2    Damoc, C.3    Phinney, B.S.4    Inoue, K.5
  • 80
    • 2442623298 scopus 로고    scopus 로고
    • Toc159 is a selective transit peptide receptor for the import of nucleus-encoded chloroplast proteins
    • Smith MD, Rounds CM, Wang F, Chen K, Afitlhile M, Schnell DJ. 2004. at Toc159 is a selective transit peptide receptor for the import of nucleus-encoded chloroplast proteins. The Journal of Cell Biology 165:323–334. doi: 10.1083/jcb.200311074
    • (2004) The Journal of Cell Biology , vol.165 , pp. 323-334
    • Smith, M.D.1    Rounds, C.M.2    Wang, F.3    Chen, K.4    Afitlhile, M.5    Schnell, D.J.6
  • 84
    • 0034813188 scopus 로고    scopus 로고
    • Leaf-specific upregulation of chloroplast translocon genes by a CCT motif-containing protein, CIA 2
    • Sun CW, Chen LJ, Lin LC, Li HM. 2001. Leaf-specific upregulation of chloroplast translocon genes by a CCT motif-containing protein, CIA 2. The Plant Cell 13:2053–2061. doi: 10.1105/tpc.13.9.2053
    • (2001) The Plant Cell , vol.13 , pp. 2053-2061
    • Sun, C.W.1    Chen, L.J.2    Lin, L.C.3    Li, H.M.4
  • 85
    • 0342332285 scopus 로고
    • Changes in photosynthesis and other chloroplast traits in lanceolate leaflet isoline of soybean
    • Sung FJ, Chen JJ. 1989. Changes in photosynthesis and other chloroplast traits in lanceolate leaflet isoline of soybean. Plant Physiology 90:773–777. doi: 10.1104/pp.90.2.773
    • (1989) Plant Physiology , vol.90 , pp. 773-777
    • Sung, F.J.1    Chen, J.J.2
  • 86
    • 0033832929 scopus 로고    scopus 로고
    • Topology studies of the chloroplast protein import channel Toc75
    • Sveshnikova N, Grimm R, Soll J, Schleiff E. 2000. Topology studies of the chloroplast protein import channel Toc75. Biological Chemistry 381:687–693. doi: 10.1515/BC.2000.089
    • (2000) Biological Chemistry , vol.381 , pp. 687-693
    • Sveshnikova, N.1    Grimm, R.2    Soll, J.3    Schleiff, E.4
  • 87
    • 84860893963 scopus 로고    scopus 로고
    • Neofunctionalization within the Omp85 protein superfamily during chloroplast evolution
    • Töpel M, Ling Q, Jarvis P. 2012. Neofunctionalization within the Omp85 protein superfamily during chloroplast evolution. Plant Signaling & Behavior 7:161–164. doi: 10.4161/psb.18677
    • (2012) Plant Signaling & Behavior , vol.7 , pp. 161-164
    • Töpel, M.1    Ling, Q.2    Jarvis, P.3
  • 88
    • 0030293036 scopus 로고    scopus 로고
    • A novel, bipartite transit peptide targets OEP75 to the outer membrane of the chloroplastic envelope
    • Tranel PJ, Keegstra K. 1996. A novel, bipartite transit peptide targets OEP75 to the outer membrane of the chloroplastic envelope. The Plant Cell 8:2093–2104. doi: 10.1105/tpc.8.11.2093
    • (1996) The Plant Cell , vol.8 , pp. 2093-2104
    • Tranel, P.J.1    Keegstra, K.2
  • 91
    • 0037428132 scopus 로고    scopus 로고
    • Role of a highly conserved bacterial protein in outer membrane protein assembly
    • Voulhoux R, Bos MP, Geurtsen J, Mols M, Tommassen J. 2003. Role of a highly conserved bacterial protein in outer membrane protein assembly. Science (New York, N.Y.) 299:262–265. doi: 10.1126/science.1078973
    • (2003) Science (New York, N.Y.) , vol.299 , pp. 262-265
    • Voulhoux, R.1    Bos, M.P.2    Geurtsen, J.3    Mols, M.4    Tommassen, J.5
  • 92
    • 1842471109 scopus 로고    scopus 로고
    • Omp85, an evolutionarily conserved bacterial protein involved in outer-membrane-protein assembly
    • Voulhoux R, Tommassen J. 2004. Omp85, an evolutionarily conserved bacterial protein involved in outer-membrane-protein assembly. Research in Microbiology 155:129–135. doi: 10.1016/j.resmic.2003.11.007
    • (2004) Research in Microbiology , vol.155 , pp. 129-135
    • Voulhoux, R.1    Tommassen, J.2
  • 93
    • 0242582449 scopus 로고    scopus 로고
    • The roles of toc34 and toc75 in targeting the toc159 preprotein receptor to chloroplasts
    • Wallas TR, Smith MD, Sanchez-Nieto S, Schnell DJ. 2003. The roles of toc34 and toc75 in targeting the toc159 preprotein receptor to chloroplasts. The Journal of Biological Chemistry 278:44289–44297. doi: 10.1074/jbc.M307873200
    • (2003) The Journal of Biological Chemistry , vol.278 , pp. 44289-44297
    • Wallas, T.R.1    Smith, M.D.2    Sanchez-Nieto, S.3    Schnell, D.J.4
  • 94
    • 53749097731 scopus 로고    scopus 로고
    • The role of GTP binding and hydrolysis at the atToc159 preprotein receptor during protein import into chloroplasts
    • Wang F, Agne B, Kessler F, Schnell DJ. 2008. The role of GTP binding and hydrolysis at the atToc159 preprotein receptor during protein import into chloroplasts. The Journal of Cell Biology 183:87–99. doi: 10.1083/jcb.200803034
    • (2008) The Journal of Cell Biology , vol.183 , pp. 87-99
    • Wang, F.1    Agne, B.2    Kessler, F.3    Schnell, D.J.4
  • 95
    • 17444381980 scopus 로고    scopus 로고
    • Identification of a multicomponent complex required for outer membrane biogenesis in Escherichia coli
    • Wu T, Malinverni J, Ruiz N, Kim S, Silhavy TJ, Kahne D. 2005. Identification of a multicomponent complex required for outer membrane biogenesis in Escherichia coli. Cell 121:235–245. doi: 10.1016/j.cell.2005.02.015
    • (2005) Cell , vol.121 , pp. 235-245
    • Wu, T.1    Malinverni, J.2    Ruiz, N.3    Kim, S.4    Silhavy, T.J.5    Kahne, D.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.