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Volumn 22, Issue 1-2, 2005, Pages 73-86

Evolution of the general protein import pathway of plastids

Author keywords

Cyanobacteria; Endosymbiosis; Plastids; Protein transport; Red alga

Indexed keywords

BACTERIAL PROTEIN; CARRIER PROTEIN; CHAPERONE; OUTER MEMBRANE PROTEIN; PEPTIDASE; PROTEIN OMP85; PROTEIN TIC20; PROTEIN TIC22; PROTEIN TIC32; PROTEIN TIC40; PROTEIN TIC62; PROTEIN TOC159; PROTEIN TOC34; PROTEIN TOC64; PROTEIN TOC75; UNCLASSIFIED DRUG;

EID: 18844426261     PISSN: 09687688     EISSN: 14645203     Source Type: Journal    
DOI: 10.1080/09687860500041916     Document Type: Review
Times cited : (109)

References (75)
  • 1
    • 0034649566 scopus 로고    scopus 로고
    • Analysis of the genome sequence of the flowering plant Arabidopsis thaliana
    • Arabidopsis Genome Initiative, The. 2000. Analysis of the genome sequence of the flowering plant Arabidopsis thaliana. Nature 408:796-815.
    • (2000) Nature , vol.408 , pp. 796-815
  • 3
    • 0034507718 scopus 로고    scopus 로고
    • NADPH:Protochlorophyllide oxidoreductase uses the general import route into chloroplasts
    • Aronsson H, Sohrt K, Soil J. 2000. NADPH:Protochlorophyllide oxidoreductase uses the general import route into chloroplasts. Biol Chem 381:1263-1267.
    • (2000) Biol Chem , vol.381 , pp. 1263-1267
    • Aronsson, H.1    Sohrt, K.2    Soil, J.3
  • 4
    • 6344272089 scopus 로고    scopus 로고
    • Toc12, a novel subunit of the intermembrane space preprotein translocon of chloroplasts
    • Becker T, Hritz J, Vogel M, Caliebe A, Bukau B, Soll J, Schleiff E. 2004. Toc12, a novel subunit of the intermembrane space preprotein translocon of chloroplasts. Mol Biol Cell 15:5130-5144.
    • (2004) Mol Biol Cell , vol.15 , pp. 5130-5144
    • Becker, T.1    Hritz, J.2    Vogel, M.3    Caliebe, A.4    Bukau, B.5    Soll, J.6    Schleiff, E.7
  • 5
    • 0034076858 scopus 로고    scopus 로고
    • Why mitochondrial genes are most often found in nuclei
    • Berg OG, Kurland CG. 2000. Why mitochondrial genes are most often found in nuclei. Mol Biol Evol 17:951-961.
    • (2000) Mol Biol Evol , vol.17 , pp. 951-961
    • Berg, O.G.1    Kurland, C.G.2
  • 6
    • 0034237205 scopus 로고    scopus 로고
    • Organellar genes: Why do they end up in the nucleus?
    • Blanchard JL, Lynch M. 2000. Organellar genes: Why do they end up in the nucleus? Trends Genet 16:315-320.
    • (2000) Trends Genet , vol.16 , pp. 315-320
    • Blanchard, J.L.1    Lynch, M.2
  • 8
    • 3042554408 scopus 로고    scopus 로고
    • Identification of an OMP required for the transport of lipopolysaccharide to the bacterial cell surface
    • Bos MP, Tefsen B, Geurtsen J, Tommassen J. 2004. Identification of an OMP required for the transport of lipopolysaccharide to the bacterial cell surface. Proc Natl Acad Sci (USA) 101:9417-9422.
    • (2004) Proc Natl Acad Sci (USA) , vol.101 , pp. 9417-9422
    • Bos, M.P.1    Tefsen, B.2    Geurtsen, J.3    Tommassen, J.4
  • 9
    • 0035852227 scopus 로고    scopus 로고
    • The paradox of transit peptides; conservation of function despite divergence in primary structure
    • Bruce BD. 2001. The paradox of transit peptides; conservation of function despite divergence in primary structure. Biochim Biophys Acta 1541:2-21.
    • (2001) Biochim Biophys Acta , vol.1541 , pp. 2-21
    • Bruce, B.D.1
  • 10
    • 0031463305 scopus 로고    scopus 로고
    • The chloroplastic protein import machinery contains a Rieske-type iron-sulfur cluster and a mononuclear iron-binding protein
    • Caliebe A, Grimm R, Kaiser G, Lübeck J, Soll J, Heins L. 1997. The chloroplastic protein import machinery contains a Rieske-type iron-sulfur cluster and a mononuclear iron-binding protein. EMBO J 16:7342-7350.
    • (1997) EMBO J , vol.16 , pp. 7342-7350
    • Caliebe, A.1    Grimm, R.2    Kaiser, G.3    Lübeck, J.4    Soll, J.5    Heins, L.6
  • 11
    • 0034177573 scopus 로고    scopus 로고
    • Membrane heredity and early chloroplast evolution
    • Cavalier-Smith T. 2000. Membrane heredity and early chloroplast evolution. Trends Plant Sci 5:174-182.
    • (2000) Trends Plant Sci , vol.5 , pp. 174-182
    • Cavalier-Smith, T.1
  • 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. Plant Cell 14:641-654.
    • (2002) Plant Cell , vol.14 , pp. 641-654
    • Chen, X.1    Smith, M.D.2    Fitzpatrick, L.3    Schnell, D.J.4
  • 13
    • 1642532372 scopus 로고    scopus 로고
    • A plant outer mitochondrial membrane protein with high amino acid sequence identity to a chloroplast protein import receptor
    • Chew O, Lister R, Qbadou S, Heazlewood JL, Soll J, Schleiff E, Millar AH, Whelan J. 2004. A plant outer mitochondrial membrane protein with high amino acid sequence identity to a chloroplast protein import receptor. FEBS Lett 557:109-114.
    • (2004) FEBS Lett , vol.557 , pp. 109-114
    • Chew, O.1    Lister, R.2    Qbadou, S.3    Heazlewood, J.L.4    Soll, J.5    Schleiff, E.6    Millar, A.H.7    Whelan, J.8
  • 16
    • 0034697980 scopus 로고    scopus 로고
    • Predicting subcellular localization of proteins based on their N-terminal amino acid sequence
    • Emanuelsson O, Nielsen H, Brunak S, von Heijne G. 2000. Predicting subcellular localization of proteins based on their N-terminal amino acid sequence. J Mol Biol 300:1005-1016.
    • (2000) J Mol Biol , vol.300 , pp. 1005-1016
    • Emanuelsson, O.1    Nielsen, H.2    Brunak, S.3    Von Heijne, G.4
  • 17
    • 0036010858 scopus 로고    scopus 로고
    • The Slr0924 protein of Synechocystis sp. strain PCC 6803 resembles a subunit of the chloroplast protein import complex and is mainly localized in the thylakoid lumen
    • Fulda S, Norling B, Schoor A, Hagemann M. 2002. The Slr0924 protein of Synechocystis sp. strain PCC 6803 resembles a subunit of the chloroplast protein import complex and is mainly localized in the thylakoid lumen. Plant Mol Biol 49:107-118.
    • (2002) Plant Mol Biol , vol.49 , pp. 107-118
    • Fulda, S.1    Norling, B.2    Schoor, A.3    Hagemann, M.4
  • 18
    • 0344942599 scopus 로고    scopus 로고
    • The Omp85 protein of Neisseria meningitidis is required for lipid export to the outer membrane
    • Genevrois S, Steeghs L, Roholl P, Letesson JJ, van der Ley P. 2003. The Omp85 protein of Neisseria meningitidis is required for lipid export to the outer membrane. EMBO J 22:1780-1789.
    • (2003) EMBO J , vol.22 , pp. 1780-1789
    • Genevrois, S.1    Steeghs, L.2    Roholl, P.3    Letesson, J.J.4    Van Der Ley, P.5
  • 19
    • 0033525788 scopus 로고    scopus 로고
    • Mitochondrial evolution
    • Gray MW, Burger G, Lang BF. 1999. Mitochondrial evolution. Science 283:1476-1481.
    • (1999) Science , vol.283 , pp. 1476-1481
    • Gray, M.W.1    Burger, G.2    Lang, B.F.3
  • 20
    • 0032510319 scopus 로고    scopus 로고
    • Chloroplast biogenesis: Mixing the prokaryotic and the eukaryotic?
    • Heins L, Soil J. 1998. Chloroplast biogenesis: mixing the prokaryotic and the eukaryotic? Curr Biol 8:R215-R217.
    • (1998) Curr Biol , vol.8
    • Heins, L.1    Soil, J.2
  • 22
    • 0034547870 scopus 로고    scopus 로고
    • Autotransporter proteins, evolution and redefining protein secretion: Response
    • Henderson IR, Cappello R, Nataro JP. 2000. Autotransporter proteins, evolution and redefining protein secretion: response. Trends Microbiol 8:534-535.
    • (2000) Trends Microbiol , vol.8 , pp. 534-535
    • Henderson, I.R.1    Cappello, R.2    Nataro, J.P.3
  • 23
    • 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. Biophys J 83:899-911.
    • (2002) Biophys J , vol.83 , pp. 899-911
    • Hinnah, S.C.1    Wagner, R.2    Sveshnikova, N.3    Harrer, R.4    Soll, J.5
  • 24
    • 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 NR, Theg SM. 2003. Physcomitrella patens as a model for the study of chloroplast protein transport: conserved machineries between vascular and non-vascular plants. Plant Mol Biol 53:621-632.
    • (2003) Plant Mol Biol , vol.53 , pp. 621-632
    • Hofmann, N.R.1    Theg, S.M.2
  • 26
    • 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. Plant J 34:661-669.
    • (2003) Plant J , vol.34 , pp. 661-669
    • Inoue, K.1    Keegstra, K.2
  • 27
    • 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. Eur J Biochem 268:4036-4043.
    • (2001) Eur J Biochem , vol.268 , pp. 4036-4043
    • Inoue, K.1    Demel, R.2    De Kruijff, B.3    Keegstra, K.4
  • 28
    • 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. Plant J 39:354-365.
    • (2004) Plant J , vol.39 , pp. 354-365
    • Inoue, K.1    Potter, D.2
  • 29
    • 0032568826 scopus 로고    scopus 로고
    • The hydrophilic domain of Tic110, an inner envelope membrane component of the chloroplastic protein translocation apparatus, faces the stromal compartment
    • Jackson DT, Froehlich JE, Keegstra K. 1998. The hydrophilic domain of Tic110, an inner envelope membrane component of the chloroplastic protein translocation apparatus, faces the stromal compartment. J Biol Chem 273:16583-16588.
    • (1998) J Biol Chem , vol.273 , pp. 16583-16588
    • Jackson, D.T.1    Froehlich, J.E.2    Keegstra, K.3
  • 30
    • 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 Physiol 125:1567-1576.
    • (2001) Plant Physiol , vol.125 , pp. 1567-1576
    • Jackson-Constan, D.1    Keegstra, K.2
  • 31
    • 0035035580 scopus 로고    scopus 로고
    • Two-partner secretion in Gram-negative bacteria: A thrifty, specific pathway for large virulence proteins
    • Jacob-Dubuisson F, Locht C, Antoine R. 2001. Two-partner secretion in Gram-negative bacteria: a thrifty, specific pathway for large virulence proteins. Mol Microbiol 40:306-313.
    • (2001) Mol Microbiol , vol.40 , pp. 306-313
    • Jacob-Dubuisson, F.1    Locht, C.2    Antoine, R.3
  • 32
    • 1942477363 scopus 로고    scopus 로고
    • Organellar proteomics: Chloroplasts in the spotlight
    • Jarvis P. 2004. Organellar proteomics: chloroplasts in the spotlight. Curr Biol 14:R317-319.
    • (2004) Curr Biol , vol.14
    • Jarvis, P.1
  • 33
    • 0030606607 scopus 로고    scopus 로고
    • Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions
    • Kaneko T, Sato S, Kotani H, Tanaka A, Asamizu E, Nakamura Y, Miyajima N, Hirosawa M, Sugiura M, Sasamoto S, et al. 1996. Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions. DNA Res 3:109-136.
    • (1996) DNA Res , vol.3 , pp. 109-136
    • Kaneko, T.1    Sato, S.2    Kotani, H.3    Tanaka, A.4    Asamizu, E.5    Nakamura, Y.6    Miyajima, N.7    Hirosawa, M.8    Sugiura, M.9    Sasamoto, S.10
  • 34
    • 0033117218 scopus 로고    scopus 로고
    • Protein import and routing systems of chloroplasts
    • Keegstra K, Cline K. 1999. Protein import and routing systems of chloroplasts. Plant Cell 11:557-570.
    • (1999) Plant Cell , vol.11 , pp. 557-570
    • Keegstra, K.1    Cline, K.2
  • 35
    • 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 Cell Biol 14:334-338.
    • (2004) Trends Cell Biol , vol.14 , pp. 334-338
    • Kessler, F.1    Schnell, D.J.2
  • 36
    • 0842313317 scopus 로고    scopus 로고
    • Substrate-dependent and organ-specific chloroplast protein import in planta
    • Kim C, Apel K. 2004. Substrate-dependent and organ-specific chloroplast protein import in planta. Plant Cell 16:88-98.
    • (2004) Plant Cell , vol.16 , pp. 88-98
    • Kim, C.1    Apel, K.2
  • 37
    • 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. J Cell Biol 143:991-1002.
    • (1998) J Cell Biol , vol.143 , pp. 991-1002
    • Kouranov, A.1    Chen, X.2    Fuks, B.3    Schnell, D.J.4
  • 38
    • 0037112789 scopus 로고    scopus 로고
    • Protein import into chloroplasts involves redox-regulated proteins
    • Küchler M, Decker S, Hörmann F, Soll J, Heins L. 2002. Protein import into chloroplasts involves redox-regulated proteins. EMBO J 21:6136-6145.
    • (2002) EMBO J , vol.21 , pp. 6136-6145
    • Küchler, M.1    Decker, S.2    Hörmann, F.3    Soll, J.4    Heins, L.5
  • 39
    • 0345299175 scopus 로고    scopus 로고
    • Metabolic symbiosis at the origin of eukaryotes
    • Lopez-Garcia P, Moreira D. 1999. Metabolic symbiosis at the origin of eukaryotes. Trends Biochem Sci 24:88-93.
    • (1999) Trends Biochem Sci , vol.24 , pp. 88-93
    • Lopez-Garcia, P.1    Moreira, D.2
  • 40
    • 0042307520 scopus 로고    scopus 로고
    • Gene transfer from organelles to the nucleus: Frequent and in big chunks
    • Martin W. 2003. Gene transfer from organelles to the nucleus: frequent and in big chunks. Proc Natl Acad Sci (USA) 100:8612-8614.
    • (2003) Proc Natl Acad Sci (USA) , vol.100 , pp. 8612-8614
    • Martin, W.1
  • 41
    • 0037126071 scopus 로고    scopus 로고
    • Evolutionary analysis of Arabidopsis, cyanobacterial, and chloroplast genomes reveals plastid phylogeny and thousands of cyanobacterial genes in the nucleus
    • Martin W, Rujan T, Richly E, Hansen A, Cornelsen S, Lins T, Leister D, Stoebe B, Hasegawa M, Penny D. 2002. Evolutionary analysis of Arabidopsis, cyanobacterial, and chloroplast genomes reveals plastid phylogeny and thousands of cyanobacterial genes in the nucleus. Proc Natl Acad Sci (USA) 99:12246-12251.
    • (2002) Proc Natl Acad Sci (USA) , vol.99 , pp. 12246-12251
    • Martin, W.1    Rujan, T.2    Richly, E.3    Hansen, A.4    Cornelsen, S.5    Lins, T.6    Leister, D.7    Stoebe, B.8    Hasegawa, M.9    Penny, D.10
  • 43
    • 3142738371 scopus 로고    scopus 로고
    • Evolution: Red algal genome affirms a common origin of all plastids
    • McFadden GI, van Dooren GG. 2004. Evolution: red algal genome affirms a common origin of all plastids. Curr Biol 14:R514-R516.
    • (2004) Curr Biol , vol.14
    • McFadden, G.I.1    Van Dooren, G.G.2
  • 44
    • 18844442890 scopus 로고    scopus 로고
    • The Tat pathway in bacteria and chloroplasts
    • Müller M, Klösgen RB. 2005. The Tat pathway in bacteria and chloroplasts (Review). Mol Membr Biol 22: 113-121.
    • (2005) Mol Membr Biol , vol.22 , pp. 113-121
    • Müller, M.1    Klösgen, R.B.2
  • 46
    • 18844387083 scopus 로고    scopus 로고
    • Signal recognition particles in chloroplasts, bacteria, yeast and mammals
    • Pool M. 2005. Signal recognition particles in chloroplasts, bacteria, yeast and mammals (Review). Mol Membr Biol 22: 3-15.
    • (2005) Mol Membr Biol , vol.22 , pp. 3-15
    • Pool, M.1
  • 48
    • 1242319241 scopus 로고    scopus 로고
    • Identification of plastid envelope proteins required for import of protochlorophyllide oxidoreductase A into the chloroplast of barley
    • Reinbothe S, Quigley F, Gray J, Schemenewitz A, Reinbothe C. 2004. Identification of plastid envelope proteins required for import of protochlorophyllide oxidoreductase A into the chloroplast of barley. Proc Natl Acad Sci (USA) 101:2197-2202.
    • (2004) Proc Natl Acad Sci (USA) , vol.101 , pp. 2197-2202
    • Reinbothe, S.1    Quigley, F.2    Gray, J.3    Schemenewitz, A.4    Reinbothe, C.5
  • 49
    • 0033179289 scopus 로고    scopus 로고
    • The endosymbiotic origin of the protein import machinery of chloroplastic envelope membranes
    • Reumann S, Keegstra K. 1999. The endosymbiotic origin of the protein import machinery of chloroplastic envelope membranes. Trends Plant Sci 4:302-307.
    • (1999) Trends Plant Sci , vol.4 , pp. 302-307
    • Reumann, S.1    Keegstra, K.2
  • 50
    • 0033582158 scopus 로고    scopus 로고
    • The evolutionary origin of the protein-translocating channel of chloroplastic envelope membranes: Identification of a cyanobacterial homolog
    • Reumann S, Davila-Aponte J, Keegstra K. 1999. The evolutionary origin of the protein-translocating channel of chloroplastic envelope membranes: identification of a cyanobacterial homolog. Proc Natl Acad Sci (USA) 96:784-789.
    • (1999) Proc Natl Acad Sci (USA) , vol.96 , pp. 784-789
    • Reumann, S.1    Davila-Aponte, J.2    Keegstra, K.3
  • 51
    • 1642276286 scopus 로고    scopus 로고
    • An improved prediction of chloroplast proteins reveals diversities and commonalities in the chloroplast proteomes of Arabidopsis and rice
    • Richly E, Leister D. 2004. An improved prediction of chloroplast proteins reveals diversities and commonalities in the chloroplast proteomes of Arabidopsis and rice. Gene 329:11-16.
    • (2004) Gene , vol.329 , pp. 11-16
    • Richly, E.1    Leister, D.2
  • 52
    • 0032560485 scopus 로고    scopus 로고
    • A chloroplast processing enzyme functions as the general stromal processing peptidase
    • Richter S, Lamppa GK. 1998. A chloroplast processing enzyme functions as the general stromal processing peptidase. Proc Natl Acad Sci (USA) 95:7463-7468.
    • (1998) Proc Natl Acad Sci (USA) , vol.95 , pp. 7463-7468
    • Richter, S.1    Lamppa, G.K.2
  • 53
    • 0642377467 scopus 로고    scopus 로고
    • POTRA: A conserved domain in the FtsQ family and a class of beta-barrel outer membrane proteins
    • Sanchez-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 Biochem Sci 28:523-526.
    • (2003) Trends Biochem Sci , vol.28 , pp. 523-526
    • Sanchez-Pulido, L.1    Devos, D.2    Genevrois, S.3    Vicente, M.4    Valencia, A.5
  • 54
    • 0035852243 scopus 로고    scopus 로고
    • Without a little help from 'my' friend: Direct insertion of proteins into chloroplast membranes?
    • Schleiff E, Klösgen RB. 2001. Without a little help from 'my' friend: Direct insertion of proteins into chloroplast membranes? Biochim Biophys Acta 1541:22-33.
    • (2001) Biochim Biophys Acta , vol.1541 , pp. 22-33
    • Schleiff, E.1    Klösgen, R.B.2
  • 55
    • 0037379183 scopus 로고    scopus 로고
    • Prediction of the plant beta-barrel proteome: A case study of the chloroplast outer envelope
    • Schleiff E, Eichacker LA, Eckart K, Becker T, Mirus O, Stahl T, Soll J. 2003a. Prediction of the plant beta-barrel proteome: a case study of the chloroplast outer envelope. Protein Sci 12:748-759.
    • (2003) Protein Sci , vol.12 , pp. 748-759
    • Schleiff, E.1    Eichacker, L.A.2    Eckart, K.3    Becker, T.4    Mirus, O.5    Stahl, T.6    Soll, J.7
  • 56
    • 0037450662 scopus 로고    scopus 로고
    • Characterization of the translocon of the outer envelope of chloroplasts
    • Schleiff E, Soil J, Kuchler M, Kuhlbrandt W, Harrer R. 2003b. Characterization of the translocon of the outer envelope of chloroplasts. J Cell Biol 160:541-551.
    • (2003) J Cell Biol , vol.160 , pp. 541-551
    • Schleiff, E.1    Soil, J.2    Kuchler, M.3    Kuhlbrandt, W.4    Harrer, R.5
  • 57
    • 0000103040 scopus 로고    scopus 로고
    • A consensus nomenclature for the protein-import components of the chloroplast envelope
    • Schnell DJ, Blobel G, Keegstra K, Kessler F, Ko K, Soll J. 1997. A consensus nomenclature for the protein-import components of the chloroplast envelope. Trends Cell Biol 7:303-304.
    • (1997) Trends Cell Biol , vol.7 , pp. 303-304
    • Schnell, D.J.1    Blobel, G.2    Keegstra, K.3    Kessler, F.4    Ko, K.5    Soll, J.6
  • 58
    • 0037459073 scopus 로고    scopus 로고
    • Protein translocons: Multifunctional mediators of protein translocation across membranes
    • Schnell DJ, Hebert DN. 2003. Protein translocons: multifunctional mediators of protein translocation across membranes. Cell 112:491-505.
    • (2003) Cell , vol.112 , pp. 491-505
    • Schnell, D.J.1    Hebert, D.N.2
  • 59
    • 0035984030 scopus 로고    scopus 로고
    • The treasure trove of algal chloroplast genomes. Surprises in architecture and gene content, and their functional implications
    • Simpson CL, Stern DB. 2002. The treasure trove of algal chloroplast genomes. Surprises in architecture and gene content, and their functional implications. Plant Physiol 129:957-966.
    • (2002) Plant Physiol , vol.129 , pp. 957-966
    • Simpson, C.L.1    Stern, D.B.2
  • 60
    • 0034689055 scopus 로고    scopus 로고
    • Toc64, a new component of the protein translocon of chloroplasts
    • Sohrt K, Soil J. 2000. Toc64, a new component of the protein translocon of chloroplasts. J Cell Biol 148:1213-1221.
    • (2000) J Cell Biol , vol.148 , pp. 1213-1221
    • Sohrt, K.1    Soil, J.2
  • 61
  • 62
    • 0033601180 scopus 로고    scopus 로고
    • Tic40, a new 'old' subunit of the chloroplast protein import translocon
    • Stahl T, Glockmann C, Soll J, Heins L. 1999. Tic40, a new 'old' subunit of the chloroplast protein import translocon. J Biol Chem 274:37467-37472.
    • (1999) J Biol Chem , vol.274 , pp. 37467-37472
    • Stahl, T.1    Glockmann, C.2    Soll, J.3    Heins, L.4
  • 63
    • 18844400862 scopus 로고    scopus 로고
    • Protein translocation into and within cyanelles
    • Steiner JM, Löffelhardt W. 2005. Protein translocation into and within cyanelles (Review). Mol Membr Biol 22: 123-132.
    • (2005) Mol Membr Biol , vol.22 , pp. 123-132
    • Steiner, J.M.1    Löffelhardt, W.2
  • 64
    • 0029434954 scopus 로고
    • The chloroplast genome
    • Sugiura M. 1995. The chloroplast genome. Essays Biochem 30:49-57.
    • (1995) Essays Biochem , vol.30 , pp. 49-57
    • Sugiura, M.1
  • 65
    • 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. Biol Chem 381:687-693.
    • (2000) Biol Chem , vol.381 , pp. 687-693
    • Sveshnikova, N.1    Grimm, R.2    Soll, J.3    Schleiff, E.4
  • 66
    • 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. Plant Cell 8:2093-2104.
    • (1996) Plant Cell , vol.8 , pp. 2093-2104
    • Tranel, P.J.1    Keegstra, K.2
  • 67
    • 0029053516 scopus 로고
    • A component of the chloroplastic protein import apparatus is targeted to the outer envelope membrane via a novel pathway
    • Tranel PJ, Froehlich J, Goyal A, Keegstra K. 1995. A component of the chloroplastic protein import apparatus is targeted to the outer envelope membrane via a novel pathway. EMBO J 14:2436-2446.
    • (1995) EMBO J , vol.14 , pp. 2436-2446
    • Tranel, P.J.1    Froehlich, J.2    Goyal, A.3    Keegstra, K.4
  • 68
    • 4043067925 scopus 로고    scopus 로고
    • Import Pathways of Chloroplast Interior Proteins and the Outer-Membrane Protein OEP14 Converge at Toc75
    • Tu SL, Chen LJ, Smith MD, Su YS, Schnell DJ, Li HS. 2004. Import Pathways of Chloroplast Interior Proteins and the Outer-Membrane Protein OEP14 Converge at Toc75. Plant Cell 16:2078-2088.
    • (2004) Plant Cell , vol.16 , pp. 2078-2088
    • Tu, S.L.1    Chen, L.J.2    Smith, M.D.3    Su, Y.S.4    Schnell, D.J.5    Li, H.S.6
  • 69
    • 0033520470 scopus 로고    scopus 로고
    • The envelope anion channel involved in chloroplast protein import is associated with Tic110
    • van den Wijngaard PW, Vredenberg WJ. 1999. The envelope anion channel involved in chloroplast protein import is associated with Tic110. J Biol Chem 274:25201-25204.
    • (1999) J Biol Chem , vol.274 , pp. 25201-25204
    • Van Den Wijngaard, P.W.1    Vredenberg, W.J.2
  • 71
    • 0037189526 scopus 로고    scopus 로고
    • Processing of an apicoplast leader sequence in Plasmodium falciparum and the identification of a putative leader cleavage enzyme
    • Van Dooren GG, Su V, D'Ombrain MC, McFadden GI. 2002. Processing of an apicoplast leader sequence in Plasmodium falciparum and the identification of a putative leader cleavage enzyme. J Biol Chem 277:23612-23619.
    • (2002) J Biol Chem , vol.277 , pp. 23612-23619
    • Van Dooren, G.G.1    Su, V.2    D'Ombrain, M.C.3    McFadden, G.I.4
  • 72
    • 0028304680 scopus 로고
    • Membrane proteins: From sequence to structure
    • von Heijne G. 1994. Membrane proteins: From sequence to structure. Annu Rev Biophys Biomol Struct 23:167-192.
    • (1994) Annu Rev Biophys Biomol Struct , vol.23 , pp. 167-192
    • Von Heijne, G.1
  • 73
    • 0024542834 scopus 로고
    • Domain structure of mitochondrial and chloroplast targeting peptides
    • von Heijne G, Steppuhn J, Herrmann RG. 1989. Domain structure of mitochondrial and chloroplast targeting peptides. Eur J Biochem 180:535-545.
    • (1989) Eur J Biochem , vol.180 , pp. 535-545
    • Von Heijne, G.1    Steppuhn, J.2    Herrmann, R.G.3
  • 74
    • 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 299:262-265.
    • (2003) Science , vol.299 , pp. 262-265
    • Voulhoux, R.1    Bos, M.P.2    Geurtsen, J.3    Mols, M.4    Tommassen, J.5


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