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Volumn 5, Issue MAY, 2014, Pages

A new member of the psToc159 family contributes to distinct protein targeting pathways in pea chloroplasts

Author keywords

Chloroplast; Import; Pea; Receptor protein; Targeting

Indexed keywords


EID: 84902296731     PISSN: None     EISSN: 1664462X     Source Type: Journal    
DOI: 10.3389/fpls.2014.00239     Document Type: Article
Times cited : (14)

References (47)
  • 1
    • 77954291457 scopus 로고    scopus 로고
    • The acidic A-domain of Arabidopsis TOC159 occurs as a hyperphosphorylated protein
    • doi: 10.1104/pp.110.158048
    • Agne, B., Andres, C., Montandon, C., Christ, B., Ertan, A., Jung, F., et al. (2010). The acidic A-domain of Arabidopsis TOC159 occurs as a hyperphosphorylated protein. Plant Physiol. 153, 1016-1030. doi: 10.1104/pp.110.158048
    • (2010) Plant Physiol. , vol.153 , pp. 1016-1030
    • Agne, B.1    Andres, C.2    Montandon, C.3    Christ, B.4    Ertan, A.5    Jung, F.6
  • 3
    • 23944495607 scopus 로고    scopus 로고
    • A molecular-genetic study of the Arabidopsis Toc75 gene family
    • doi: 10.1104/pp.105.063289
    • Baldwin, A., Wardle, A., Patel, R., Dudley, P., Park, S. K., Twell, D., et al. (2005). A molecular-genetic study of the Arabidopsis Toc75 gene family. Plant Physiol. 138, 715-733. doi: 10.1104/pp.105.063289
    • (2005) Plant Physiol. , vol.138 , pp. 715-733
    • Baldwin, A.1    Wardle, A.2    Patel, R.3    Dudley, P.4    Park, S.K.5    Twell, D.6
  • 4
    • 0034642558 scopus 로고    scopus 로고
    • The major protein import receptor of plastids is essential for chloroplast biogenesis
    • doi: 10.1038/35003214
    • Bauer, J., Chen, K., Hiltbunner, A., Wehrli, E., Eugster, M., Schnell, D., et al. (2000). The major protein import receptor of plastids is essential for chloroplast biogenesis. Nature 403, 203-207. doi: 10.1038/35003214
    • (2000) Nature , vol.403 , pp. 203-207
    • Bauer, J.1    Chen, K.2    Hiltbunner, A.3    Wehrli, E.4    Eugster, M.5    Schnell, D.6
  • 5
    • 84855182246 scopus 로고    scopus 로고
    • Plastid proteome assembly without Toc159: Photosynthetic protein import and accumulation of N-acetylated plastid precursor proteins
    • doi: 10.1105/tpc.111.092882
    • Bischof, S., Baerenfaller, K., Wildhaber, T., Troesch, R., Vidi, P. A., Roschitzki, B., et al. (2011). Plastid proteome assembly without Toc159: photosynthetic protein import and accumulation of N-acetylated plastid precursor proteins. Plant Cell 23, 3911-3928. doi: 10.1105/tpc.111.092882
    • (2011) Plant Cell , vol.23 , pp. 3911-3928
    • Bischof, S.1    Baerenfaller, K.2    Wildhaber, T.3    Troesch, R.4    Vidi, P.A.5    Roschitzki, B.6
  • 6
    • 84869406456 scopus 로고    scopus 로고
    • The gateway to chloroplast: Re-defining the function of chloroplast receptor proteins
    • doi: 10.1515/hsz-2012-0235
    • Chang, W.-L., Soll, J., and Bölter, B. (2012). The gateway to chloroplast: re-defining the function of chloroplast receptor proteins. Biol. Chem. 339, 1263-1277. doi: 10.1515/hsz-2012-0235
    • (2012) Biol. Chem. , vol.339 , pp. 1263-1277
    • Chang, W.-L.1    Soll, J.2    Bölter, B.3
  • 7
    • 0032189210 scopus 로고    scopus 로고
    • A mutant deficient in the plastid lipid DGD is defective in protein import into chloroplasts
    • doi: 10.1046/j.1365-313x.1998.00270.x
    • Chen, L.-J., and Li, H.-M. (1998). A mutant deficient in the plastid lipid DGD is defective in protein import into chloroplasts. Plant J. 16, 33-39. doi: 10.1046/j.1365-313x.1998.00270.x
    • (1998) Plant J. , vol.16 , pp. 33-39
    • Chen, L.-J.1    Li, H.-M.2
  • 8
    • 0019412749 scopus 로고
    • Separation and characterization of inner and outer envelope membranes of pea chloroplasts
    • doi: 10.1073/pnas.78.6.3595
    • Cline, K., Andrews, J., Mersey, B., Newcomb, E. H., and Keegstra, K. (1981). Separation and characterization of inner and outer envelope membranes of pea chloroplasts. Proc. Natl. Acad. Sci. U.S. A 78, 3595-3599. doi: 10.1073/pnas.78.6.3595
    • (1981) Proc. Natl. Acad. Sci. U.S. A , vol.78 , pp. 3595-3599
    • Cline, K.1    Andrews, J.2    Mersey, B.3    Newcomb, E.H.4    Keegstra, K.5
  • 9
    • 77953149231 scopus 로고    scopus 로고
    • AT_CHLORO: A comprehensive chloroplast proteome database with subplastidiallocalization and curated information on envelope proteins
    • doi: 10.1074/mcp.M900325-MCP200
    • Ferro, M., Brugière, S., Salvi, D., Seigneurin-Berny, D., Court, M., Moyet, L., et al. (2010). AT_CHLORO: a comprehensive chloroplast proteome database with subplastidiallocalization and curated information on envelope proteins. Mol. Cell. Proteomics 9, 1063-1084. doi: 10.1074/mcp.M900325-MCP200
    • (2010) Mol. Cell. Proteomics , vol.9 , pp. 1063-1084
    • Ferro, M.1    Brugière, S.2    Salvi, D.3    Seigneurin-Berny, D.4    Court, M.5    Moyet, L.6
  • 10
    • 0348136190 scopus 로고    scopus 로고
    • Proteomics of the chloroplast envelope membranes from Arabidopsis thaliana
    • doi: 10.1074/mcp.M300030-MCP200
    • Ferro, M., Salvi, D., Brugiere, S., Miras, S., Kowalski, S., Louwagie, M., et al. (2003). Proteomics of the chloroplast envelope membranes from Arabidopsis thaliana. Mol. Cell. Proteomics 2, 325-345. doi: 10.1074/mcp.M300030-MCP200
    • (2003) Mol. Cell. Proteomics , vol.2 , pp. 325-345
    • Ferro, M.1    Salvi, D.2    Brugiere, S.3    Miras, S.4    Kowalski, S.5    Louwagie, M.6
  • 11
    • 0023041137 scopus 로고
    • Energy dependence of protein translocation into chloroplasts
    • doi: 10.1111/j.1432-1033.1986.tb10075.x
    • Flügge, U. I., and Hinz, G. (1986). Energy dependence of protein translocation into chloroplasts. Eur. J. Biochem. 160, 563-570. doi: 10.1111/j.1432-1033.1986.tb10075.x
    • (1986) Eur. J. Biochem. , vol.160 , pp. 563-570
    • Flügge, U.I.1    Hinz, G.2
  • 12
    • 79955769112 scopus 로고    scopus 로고
    • Comprehensive transcriptome analysis of the highly complex Pisum sativum genome using next generation sequencing
    • doi: 10.1186/1471-2164-12-227
    • Franssen, S., Shrestha, R., Brautigam, A., Bornberg-Bauer, E., and Weber, A. (2011). Comprehensive transcriptome analysis of the highly complex Pisum sativum genome using next generation sequencing. BMC Genomics 12:227. doi: 10.1186/1471-2164-12-227
    • (2011) BMC Genomics , vol.12 , pp. 227
    • Franssen, S.1    Shrestha, R.2    Brautigam, A.3    Bornberg-Bauer, E.4    Weber, A.5
  • 13
    • 0037088638 scopus 로고    scopus 로고
    • The chloroplast protein import receptors Toc34 and Toc159 are phosphorylated by distinct protein kinases
    • doi: 10.1074/jbc.M110679200
    • Fulgosi, H., and Soll, J. (2002). The chloroplast protein import receptors Toc34 and Toc159 are phosphorylated by distinct protein kinases. J. Biol. Chem. 277, 8934-8940. doi: 10.1074/jbc.M110679200
    • (2002) J. Biol. Chem. , vol.277 , pp. 8934-8940
    • Fulgosi, H.1    Soll, J.2
  • 14
    • 0033802314 scopus 로고    scopus 로고
    • Functional analysis of the two Arabidopsis homologues of Toc34, a component of the chloroplast protein import apparatus
    • doi: 10.1046/j.1365-313x.2000.00849.x
    • Gutensohn, M., Schulz, B., Nicolay, P., and Flugge, U. I. (2000). Functional analysis of the two Arabidopsis homologues of Toc34, a component of the chloroplast protein import apparatus. Plant J. 23, 771-783. doi: 10.1046/j.1365-313x.2000.00849.x
    • (2000) Plant J. , vol.23 , pp. 771-783
    • Gutensohn, M.1    Schulz, B.2    Nicolay, P.3    Flugge, U.I.4
  • 15
    • 4043084085 scopus 로고    scopus 로고
    • atToc90, a new GTP-binding component of the Arabidopsis chloroplast protein import machinery
    • doi: 10.1023/B:PLAN.0000036374.92546.51
    • Hiltbrunner, A., Grunig, K., Alvarez-Huerta, M., Infanger, S., Bauer, J., and Kessler, F. (2004). atToc90, a new GTP-binding component of the Arabidopsis chloroplast protein import machinery. Plant Mol. Biol. 54, 427-440. doi: 10.1023/B:PLAN.0000036374.92546.51
    • (2004) Plant Mol. Biol. , vol.54 , pp. 427-440
    • Hiltbrunner, A.1    Grunig, K.2    Alvarez-Huerta, M.3    Infanger, S.4    Bauer, J.5    Kessler, F.6
  • 16
    • 0031464541 scopus 로고    scopus 로고
    • Reconstitution of a chloroplast protein import channel
    • doi: 10.1093/emboj/16.24.7351
    • Hinnah, S. C., Hill, K., Wagner, R., Schlicher, T., and Soll, J. (1997). Reconstitution of a chloroplast protein import channel. EMBO J. 16, 7351-7360. doi: 10.1093/emboj/16.24.7351
    • (1997) EMBO J. , vol.16 , pp. 7351-7360
    • Hinnah, S.C.1    Hill, K.2    Wagner, R.3    Schlicher, T.4    Soll, J.5
  • 17
    • 0029257261 scopus 로고
    • Import of a new chloroplast inner envelope protein is greatly stimulated by potassium phosphate
    • doi: 10.1007/BF00020890
    • Hirsch, S., and Soll, J. (1995). Import of a new chloroplast inner envelope protein is greatly stimulated by potassium phosphate. Plant Mol. Biol. 27, 1173-1181. doi: 10.1007/BF00020890
    • (1995) Plant Mol. Biol. , vol.27 , pp. 1173-1181
    • Hirsch, S.1    Soll, J.2
  • 18
    • 1942442458 scopus 로고    scopus 로고
    • Physcomitrella patens as a model for the study of chloroplast protein transport: Conserved machineries between vascular and non-vascular plants
    • Hofmann, N. R., and Theg, S. M. (2004). Physcomitrella patens as a model for the study of chloroplast protein transport: conserved machineries between vascular and non-vascular plants. Plant Molec. Biol. 53, 621-632.
    • (2004) Plant Molec. Biol. , vol.53 , pp. 621-632
    • Hofmann, N.R.1    Theg, S.M.2
  • 19
    • 30944465751 scopus 로고    scopus 로고
    • Arabidopsis tic110 is essential for the assembly and function of the protein import machinery of plastids
    • doi: 10.1105/tpc.105.030700
    • Inaba, T., Alvarez-Huerta, M., Li, M., Bauer, J., Ewers, C., Kessler, F., et al. (2005). Arabidopsis tic110 is essential for the assembly and function of the protein import machinery of plastids. Plant Cell 17, 1482-1496. doi: 10.1105/tpc.105.030700
    • (2005) 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
  • 20
    • 77955879890 scopus 로고    scopus 로고
    • The molecular basis for distinct pathways for protein import into arabidopsis chloroplasts
    • doi: 10.1105/tpc.110.074328, 1977-1960
    • Inoue, H., Rounds, C., and Schnell, D. J. (2010). The molecular basis for distinct pathways for protein import into arabidopsis chloroplasts. Plant Cell 22, 1977-1960. doi: 10.1105/tpc.110.074328
    • (2010) Plant Cell , vol.22
    • Inoue, H.1    Rounds, C.2    Schnell, D.J.3
  • 21
    • 3042724874 scopus 로고    scopus 로고
    • Members of the Toc159 import receptor family represent distinct pathways for protein targeting to plastids
    • doi: 10.1091/mbc.E03-12-0923
    • Ivanova, Y., Smith, M. D., Chen, K., and Schnell, D. J. (2004). Members of the Toc159 import receptor family represent distinct pathways for protein targeting to plastids. Mol. Biol. Cell 15, 3379-3392. doi: 10.1091/mbc.E03-12-0923
    • (2004) Mol. Biol. Cell , vol.15 , pp. 3379-3392
    • Ivanova, Y.1    Smith, M.D.2    Chen, K.3    Schnell, D.J.4
  • 22
    • 47249152709 scopus 로고    scopus 로고
    • Targeting of nucleus-encoded proteins to chloroplasts in plants
    • doi: 10.1111/j.1469-8137.2008.02452.x
    • Jarvis, P. (2008). Targeting of nucleus-encoded proteins to chloroplasts in plants. New Phytol. 179, 257-285. doi: 10.1111/j.1469-8137.2008.02452.x
    • (2008) New Phytol. , vol.179 , pp. 257-285
    • Jarvis, P.1
  • 23
    • 0032476027 scopus 로고    scopus 로고
    • An Arabidopsis mutant defective in the plastid general protein import apparatus
    • doi: 10.1126/science.282.5386.100
    • Jarvis, P., Chen, L. J., Li, H., Peto, C. A., Fankhauser, C., and Chory, J. (1998). An Arabidopsis mutant defective in the plastid general protein import apparatus. Science 282, 100-103. doi: 10.1126/science.282.5386.100
    • (1998) Science , vol.282 , pp. 100-103
    • Jarvis, P.1    Chen, L.J.2    Li, H.3    Peto, C.A.4    Fankhauser, C.5    Chory, J.6
  • 24
    • 52049110120 scopus 로고    scopus 로고
    • The chloroplast protein translocation complexes of Chlamydomonas reinhardtii: A bioinformatic comparison of Toc and Tic components in plants, green algae and red algae
    • doi: 10.1534/genetics.107.085704
    • Kalanon, M., and McFadden, G. I. (2008). The chloroplast protein translocation complexes of Chlamydomonas reinhardtii: a bioinformatic comparison of Toc and Tic components in plants, green algae and red algae. Genetics179, 95-112. doi: 10.1534/genetics.107.085704
    • (2008) Genetics , vol.179 , pp. 95-112
    • Kalanon, M.1    McFadden, G.I.2
  • 25
    • 0033117218 scopus 로고    scopus 로고
    • Protein import and routing systems of chloroplasts
    • doi: 10.1105/tpc.11.4.557
    • Keegstra, K., and Cline, K. (1999). Protein import and routing systems of chloroplasts. Plant Cell 11, 557-570. doi: 10.1105/tpc.11.4.557
    • (1999) Plant Cell , vol.11 , pp. 557-570
    • Keegstra, K.1    Cline, K.2
  • 26
    • 0027984260 scopus 로고
    • Identification of two GTP-binding proteins in the chloroplast protein import machinery
    • doi: 10.1126/science.7973656
    • Kessler, F., Blobel, G., Patel, H. A., and Schnell, D. J. (1994). Identification of two GTP-binding proteins in the chloroplast protein import machinery. Science 266, 1035-1039. doi: 10.1126/science.7973656
    • (1994) Science , vol.266 , pp. 1035-1039
    • Kessler, F.1    Blobel, G.2    Patel, H.A.3    Schnell, D.J.4
  • 27
    • 1842432608 scopus 로고    scopus 로고
    • TheArabidopsis thaliana chloroplast proteome reveals pathway abundance and novel protein functions
    • doi: 10.1016/j.cub.2004.02.039
    • Kleffmann, T., Russenberger, D., Von Zychlinski, A., Christopher, W., Sjolander, K., Gruissem, W., et al. (2004). TheArabidopsis thaliana chloroplast proteome reveals pathway abundance and novel protein functions. Curr. Biol. 14, 354-362. doi: 10.1016/j.cub.2004.02.039
    • (2004) Curr. Biol. , vol.14 , pp. 354-362
    • Kleffmann, T.1    Russenberger, D.2    Von Zychlinski, A.3    Christopher, W.4    Sjolander, K.5    Gruissem, W.6
  • 28
    • 0031408330 scopus 로고    scopus 로고
    • Analysis of the interactions of preproteins with the import machinery over the course of protein import into chloroplasts
    • doi: 10.1083/jcb.139.7.1677
    • Kouranov, A., and Schnell, D. J. (1997). Analysis of the interactions of preproteins with the import machinery over the course of protein import into chloroplasts. J. Cell. Biol. 139, 1677-1685. doi: 10.1083/jcb.139.7.1677
    • (1997) J. Cell. Biol. , vol.139 , pp. 1677-1685
    • Kouranov, A.1    Schnell, D.J.2
  • 29
    • 4043127545 scopus 로고    scopus 로고
    • Functional specialization amongst the Arabidopsis Toc159 family of chloroplast protein import receptors
    • doi: 10.1105/tpc.104.023309
    • Kubis, S., Patel, R., Combe, J., Bedard, J., Kovacheva, S., Lilley, K., et al. (2004). Functional specialization amongst the Arabidopsis Toc159 family of chloroplast protein import receptors. Plant Cell 16, 2059-2077. doi: 10.1105/tpc.104.023309
    • (2004) Plant Cell , vol.16 , pp. 2059-2077
    • Kubis, S.1    Patel, R.2    Combe, J.3    Bedard, J.4    Kovacheva, S.5    Lilley, K.6
  • 30
    • 33646835436 scopus 로고    scopus 로고
    • Functional characterization of sequence motifs in the transit peptide of Arabidopsis small subunit of rubisco
    • doi: 10.1104/pp.105.074575
    • Lee, D. W., Lee, S., Lee, G. J., Lee, K. H., Kim, S., Cheong, G. W., et al. (2006). Functional characterization of sequence motifs in the transit peptide of Arabidopsis small subunit of rubisco. Plant Physiol. 140, 466-483. doi: 10.1104/pp.105.074575
    • (2006) Plant Physiol. , vol.140 , pp. 466-483
    • Lee, D.W.1    Lee, S.2    Lee, G.J.3    Lee, K.H.4    Kim, S.5    Cheong, G.W.6
  • 31
    • 70349225929 scopus 로고    scopus 로고
    • Multiple sequence motifs in the rubisco small subunit transit peptide independently contribute to Toc159-dependent import of proteins into chloroplasts
    • doi: 10.1104/pp.109.140673
    • Lee, D. W., Lee, S., Oh, Y. J., and Hwang, I. (2009). Multiple sequence motifs in the rubisco small subunit transit peptide independently contribute to Toc159-dependent import of proteins into chloroplasts. Plant Physiol. 151, 129-141. doi: 10.1104/pp.109.140673
    • (2009) Plant Physiol. , vol.151 , pp. 129-141
    • Lee, D.W.1    Lee, S.2    Oh, Y.J.3    Hwang, I.4
  • 32
    • 0141814967 scopus 로고    scopus 로고
    • The M domain of atToc159 plays an essential role in the import of proteins into chloroplasts and chloroplast biogenesis
    • doi: 10.1074/jbc.M304457200
    • Lee, K. H., Kim, S. J., Lee, Y. J., Jin, J. B., and Hwang, I. (2003). The M domain of atToc159 plays an essential role in the import of proteins into chloroplasts and chloroplast biogenesis. J. Biol. Chem. 278, 36794-36805. doi: 10.1074/jbc.M304457200
    • (2003) J. Biol. Chem. , vol.278 , pp. 36794-36805
    • Lee, K.H.1    Kim, S.J.2    Lee, Y.J.3    Jin, J.B.4    Hwang, I.5
  • 33
    • 27744432391 scopus 로고    scopus 로고
    • Plastids unleashed: Their development and their integration in plant development
    • doi: 10.1387/ijdb.051997el
    • Lopez-Juez, E., and Pyke, K. A. (2005). Plastids unleashed: their development and their integration in plant development. Int. J. Dev. Biol. 49, 557-577. doi: 10.1387/ijdb.051997el
    • (2005) Int. J. Dev. Biol. , vol.49 , pp. 557-577
    • Lopez-Juez, E.1    Pyke, K.A.2
  • 34
    • 0037033102 scopus 로고    scopus 로고
    • Non-canonical transit peptide for import into the chloroplast
    • doi: 10.1074/jbc.M207477200
    • Miras, S., Salvi, D., Ferro, M., Grunwald, D., Garin, J., Joyard, J., et al. (2002). Non-canonical transit peptide for import into the chloroplast. J. Biol. Chem. 277, 47770-47778. doi: 10.1074/jbc.M207477200
    • (2002) J. Biol. Chem. , vol.277 , pp. 47770-47778
    • Miras, S.1    Salvi, D.2    Ferro, M.3    Grunwald, D.4    Garin, J.5    Joyard, J.6
  • 35
    • 35748972640 scopus 로고    scopus 로고
    • Toc159-and Toc75-independent import of a transit sequence-less precursor into the inner envelope of chloroplasts
    • doi: 10.1074/jbc.M611112200
    • Miras, S., Salvi, D., Piette, L., Seigneurin-Berny, D., Grunwald, D., Reinbothe, C., et al. (2007). Toc159-and Toc75-independent import of a transit sequence-less precursor into the inner envelope of chloroplasts. J. Biol. Chem. 282, 29482-29492. doi: 10.1074/jbc.M611112200
    • (2007) J. Biol. Chem. , vol.282 , pp. 29482-29492
    • Miras, S.1    Salvi, D.2    Piette, L.3    Seigneurin-Berny, D.4    Grunwald, D.5    Reinbothe, C.6
  • 36
    • 4444230596 scopus 로고    scopus 로고
    • Inner envelope protein 32 is imported into chloroplasts by a novel pathway
    • doi: 10.1242/jcs.01265
    • Nada, A., and Soll, J. (2004). Inner envelope protein 32 is imported into chloroplasts by a novel pathway. J. Cell Sci. 117, 3975-3982. doi: 10.1242/jcs.01265
    • (2004) J. Cell Sci. , vol.117 , pp. 3975-3982
    • Nada, A.1    Soll, J.2
  • 37
    • 0023336093 scopus 로고
    • Protein import into chloroplasts requires a chloroplast ATPase
    • doi: 10.1073/pnas.84.10.3288
    • Pain, D., and Blobel, G. (1987). Protein import into chloroplasts requires a chloroplast ATPase. Proc. Natl. Acad. Sci. U.S. A 84, 3288-3292. doi: 10.1073/pnas.84.10.3288
    • (1987) Proc. Natl. Acad. Sci. U.S. A , vol.84 , pp. 3288-3292
    • Pain, D.1    Blobel, G.2
  • 38
    • 0027953126 scopus 로고
    • Envelope membrane proteins that interact with chloroplastic precursor proteins
    • doi: 10.1105/tpc.6.1.93
    • Perry, S. E., and Keegstra, K. (1994). Envelope membrane proteins that interact with chloroplastic precursor proteins. Plant Cell 6, 93-105. doi: 10.1105/tpc.6.1.93
    • (1994) Plant Cell , vol.6 , pp. 93-105
    • Perry, S.E.1    Keegstra, K.2
  • 39
    • 0037447068 scopus 로고    scopus 로고
    • A GTP-driven motor moves proteins across the outer envelope of chloroplasts
    • doi: 10.1073/pnas.0730860100
    • Schleiff, E., Jelic, M., and Soll, J. (2003). A GTP-driven motor moves proteins across the outer envelope of chloroplasts. Proc. Natl. Acad. Sci. U.S. A 100, 4604-4609. doi: 10.1073/pnas.0730860100
    • (2003) Proc. Natl. Acad. Sci. U.S. A , vol.100 , pp. 4604-4609
    • Schleiff, E.1    Jelic, M.2    Soll, J.3
  • 40
    • 0028109712 scopus 로고
    • Isolation of components of the chloroplast protein import machinery
    • doi: 10.1126/science.7973649
    • Schnell, D. J., Kessler, F., and Blobel, G. (1994). Isolation of components of the chloroplast protein import machinery. Science 266, 1007-1012. doi: 10.1126/science.7973649
    • (1994) Science , vol.266 , pp. 1007-1012
    • Schnell, D.J.1    Kessler, F.2    Blobel, G.3
  • 41
    • 0029257229 scopus 로고
    • A constituent of the chloroplast import complex represents a new type of GTP-binding protein
    • doi: 10.1046/j.1365-313X.1995.7030401.x
    • Seedorf, M., Waegemann, K., and Soll, J. (1995). A constituent of the chloroplast import complex represents a new type of GTP-binding protein. Plant J. 7, 401-411. doi: 10.1046/j.1365-313X.1995.7030401.x
    • (1995) Plant J. , vol.7 , pp. 401-411
    • Seedorf, M.1    Waegemann, K.2    Soll, J.3
  • 42
    • 0024978279 scopus 로고
    • Internal ATP is the only energy requirement for the translocation of precursor proteins across chloroplastic membranes
    • Theg, S. M., Bauerle, C., Olsen, L. J., Selman, B. R., and Keegstra, K. (1989). Internal ATP is the only energy requirement for the translocation of precursor proteins across chloroplastic membranes. J. Biol. Chem. 264, 6730-6736.
    • (1989) J. Biol. Chem. , vol.264 , pp. 6730-6736
    • Theg, S.M.1    Bauerle, C.2    Olsen, L.J.3    Selman, B.R.4    Keegstra, K.5
  • 43
    • 14244269889 scopus 로고    scopus 로고
    • At least two Toc34 protein import receptors with different specificities are also present in spinach chloroplasts
    • doi: 10.1016/j.febslet.2004.12.096
    • Voigt, A., Jakob, M., Klosgen, R. B., and Gutensohn, M. (2005). At least two Toc34 protein import receptors with different specificities are also present in spinach chloroplasts. FEBS Lett. 579, 1343-1349. doi: 10.1016/j.febslet.2004.12.096
    • (2005) FEBS Lett. , vol.579 , pp. 1343-1349
    • Voigt, A.1    Jakob, M.2    Klosgen, R.B.3    Gutensohn, M.4
  • 44
    • 0002147151 scopus 로고
    • Outer envelope membranes from chloroplasts are isolated as right-side-out vesicles
    • doi: 10.1007/BF00201628
    • Waegemann, K., Eichacker, S., and Soll, J. (1992). Outer envelope membranes from chloroplasts are isolated as right-side-out vesicles. Planta 187, 89-94. doi: 10.1007/BF00201628
    • (1992) Planta , vol.187 , pp. 89-94
    • Waegemann, K.1    Eichacker, S.2    Soll, J.3
  • 45
    • 0029868470 scopus 로고    scopus 로고
    • Phosphorylation of the transit sequence of chloroplast precursor proteins
    • doi: 10.1074/jbc.271.11.6545
    • Waegemann, K., and Soll, J. (1996). Phosphorylation of the transit sequence of chloroplast precursor proteins. J. Biol. Chem. 271, 6545-6554. doi: 10.1074/jbc.271.11.6545
    • (1996) J. Biol. Chem. , vol.271 , pp. 6545-6554
    • Waegemann, K.1    Soll, J.2
  • 46
    • 0033199206 scopus 로고    scopus 로고
    • GTP promotes the formation of early-import intermediates but is not required during the translocation step of protein import into chloroplasts
    • doi: 10.1104/pp.121.1.237
    • Young, M. E., Keegstra, K., and Froehlich, J. E. (1999). GTP promotes the formation of early-import intermediates but is not required during the translocation step of protein import into chloroplasts. Plant Physiol. 121, 237-244. doi: 10.1104/pp.121.1.237
    • (1999) Plant Physiol. , vol.121 , pp. 237-244
    • Young, M.E.1    Keegstra, K.2    Froehlich, J.E.3
  • 47
    • 44349099751 scopus 로고    scopus 로고
    • Sorting signals, N-terminal modifications and abundance of the chloroplast proteome
    • doi: 10.1371/journal.pone.0001994
    • Zybailov, B., Rutschow, H., Friso, G., Rudella, A., Emanuelsson, O., Sun, Q., et al. (2008). Sorting signals, N-terminal modifications and abundance of the chloroplast proteome. PLoS ONE 3:e1994. doi: 10.1371/journal.pone.0001994
    • (2008) PLoS ONE , vol.3
    • Zybailov, B.1    Rutschow, H.2    Friso, G.3    Rudella, A.4    Emanuelsson, O.5    Sun, Q.6


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