메뉴 건너뛰기




Volumn 1803, Issue 6, 2010, Pages 740-747

Protein import into chloroplasts: The Tic complex and its regulation

Author keywords

Calcium calmodulin; Chloroplast; Endosymbiosis; Protein import; Redox regulation; Tic complex

Indexed keywords

CALCIUM CALMODULIN DEPENDENT PROTEIN KINASE; CHAPERONIN; HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN 93; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; TRANSLOCON; TRANSLOCON AT THE INNER ENVELOPE MEMBRANE OF CHLOROPLAST; TRANSLOCON AT THE INNER ENVELOPE MEMBRANE OF CHLOROPLAST 110; TRANSLOCON AT THE INNER ENVELOPE MEMBRANE OF CHLOROPLAST 20; TRANSLOCON AT THE INNER ENVELOPE MEMBRANE OF CHLOROPLAST 21; TRANSLOCON AT THE INNER ENVELOPE MEMBRANE OF CHLOROPLAST 32; TRANSLOCON AT THE INNER ENVELOPE MEMBRANE OF CHLOROPLAST 40; TRANSLOCON AT THE INNER ENVELOPE MEMBRANE OF CHLOROPLAST 55; TRANSLOCON AT THE INNER ENVELOPE MEMBRANE OF CHLOROPLAST 62; TRANSLOCON AT THE OUTER ENVELOPE MEMBRANE OF CHLOROPLAST; UNCLASSIFIED DRUG;

EID: 77953022036     PISSN: 01674889     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2010.01.015     Document Type: Review
Times cited : (61)

References (96)
  • 1
    • 2942568227 scopus 로고    scopus 로고
    • A molecular timescale of eukaryote evolution and the rise of complex multicellular life
    • Hedges S.B., Blair J.E., Venturi M.L., Shoe J.L. A molecular timescale of eukaryote evolution and the rise of complex multicellular life. BMC Evol. Biol. 2004, 4:2-10.
    • (2004) BMC Evol. Biol. , vol.4 , pp. 2-10
    • Hedges, S.B.1    Blair, J.E.2    Venturi, M.L.3    Shoe, J.L.4
  • 2
    • 67649755680 scopus 로고    scopus 로고
    • Mitochondrial and plastid evolution in eukaryotes: an outsiders' perspective
    • Gross J., Bhattacharya D. Mitochondrial and plastid evolution in eukaryotes: an outsiders' perspective. Nat. Rev. Genet. 2009, 10:495-505.
    • (2009) Nat. Rev. Genet. , vol.10 , pp. 495-505
    • Gross, J.1    Bhattacharya, D.2
  • 4
    • 0034177573 scopus 로고    scopus 로고
    • Membrane heredity and early chloroplast evolution
    • Cavalier-Smith T. Membrane heredity and early chloroplast evolution. Trends Plant Sci. 2000, 5:174-182.
    • (2000) Trends Plant Sci. , vol.5 , pp. 174-182
    • Cavalier-Smith, T.1
  • 6
    • 0742323538 scopus 로고    scopus 로고
    • Endosymbiotic gene transfer: organelle genomes forge eukaryotic chromosomes
    • Timmis J.N., Ayliffe M.A., Huang C.Y., Martin W. Endosymbiotic gene transfer: organelle genomes forge eukaryotic chromosomes. Nat. Rev. Genet. 2004, 5:123-135.
    • (2004) Nat. Rev. Genet. , vol.5 , pp. 123-135
    • Timmis, J.N.1    Ayliffe, M.A.2    Huang, C.Y.3    Martin, W.4
  • 7
    • 45549100129 scopus 로고    scopus 로고
    • Reconstructing evolution: gene transfer from plastids to the nucleus
    • Bock R., Timmis J.N. Reconstructing evolution: gene transfer from plastids to the nucleus. BioEssays 2008, 30:556-566.
    • (2008) BioEssays , vol.30 , pp. 556-566
    • Bock, R.1    Timmis, J.N.2
  • 8
    • 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. Evolutionary analysis of Arabidopsis, cyanobacterial, and chloroplast genomes reveals plastid phylogeny and thousands of cyanobacterial genes in the nucleus. Proc. Nat. Acad. Sci. U. S. A. 2002, 99:12246-12251.
    • (2002) Proc. Nat. Acad. Sci. U. S. A. , 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
  • 9
    • 0037213560 scopus 로고    scopus 로고
    • Chloroplast research in the genomic age
    • Leister D. Chloroplast research in the genomic age. Trends Genet. 2003, 19:47-56.
    • (2003) Trends Genet. , vol.19 , pp. 47-56
    • Leister, D.1
  • 10
    • 34249873947 scopus 로고    scopus 로고
    • Translocation of proteins into mitochondria
    • Neupert W., Herrmann J.M. Translocation of proteins into mitochondria. Annu. Rev. Biochem. 2007, 76:723-749.
    • (2007) Annu. Rev. Biochem. , vol.76 , pp. 723-749
    • Neupert, W.1    Herrmann, J.M.2
  • 11
    • 47249152709 scopus 로고    scopus 로고
    • Targeting of nucleus-encoded proteins to chloroplasts in plants
    • Jarvis P. Targeting of nucleus-encoded proteins to chloroplasts in plants. New Phytol. 2008, 179:257-285.
    • (2008) New Phytol. , vol.179 , pp. 257-285
    • Jarvis, P.1
  • 12
    • 70349331195 scopus 로고    scopus 로고
    • Protein import machineries in endosymbiotic organelles
    • DOI: 10.10077s00018-009-8644-2
    • Balsera M., Soll J., Bölter B. Protein import machineries in endosymbiotic organelles. Cell. Mol. Life Sci. 2009, DOI: 10.10077s00018-009-8644-2.
    • (2009) Cell. Mol. Life Sci.
    • Balsera, M.1    Soll, J.2    Bölter, B.3
  • 13
    • 0034308219 scopus 로고    scopus 로고
    • Chloroplast transit peptides: structure, function and evolution
    • Bruce B.D. Chloroplast transit peptides: structure, function and evolution. Trends Cell Biol. 2000, 10:440-447.
    • (2000) Trends Cell Biol. , vol.10 , pp. 440-447
    • Bruce, B.D.1
  • 14
    • 57749094259 scopus 로고    scopus 로고
    • Arabidopsis nuclear-encoded plastid transit peptides contain multiple sequence subgroups with distinctive chloroplast-targeting sequence motifs
    • Lee D.W., Kim J.K., Lee S., Choi S., Kim S., Hwang I. Arabidopsis nuclear-encoded plastid transit peptides contain multiple sequence subgroups with distinctive chloroplast-targeting sequence motifs. Plant Cell 2008, 20:1603-1622.
    • (2008) Plant Cell , vol.20 , pp. 1603-1622
    • Lee, D.W.1    Kim, J.K.2    Lee, S.3    Choi, S.4    Kim, S.5    Hwang, I.6
  • 15
    • 0033950443 scopus 로고    scopus 로고
    • 14-3-3 proteins form a guidance complex with chloroplast precursor proteins in plants
    • May T., Soll J. 14-3-3 proteins form a guidance complex with chloroplast precursor proteins in plants. Plant Cell 2000, 12:53-64.
    • (2000) Plant Cell , vol.12 , pp. 53-64
    • May, T.1    Soll, J.2
  • 16
    • 0029868470 scopus 로고    scopus 로고
    • Phosphorylation of the transit sequence of chloroplast precursor proteins
    • Waegemann K., Soll J. Phosphorylation of the transit sequence of chloroplast precursor proteins. J. Biol. Chem. 1996, 271:6545-6554.
    • (1996) J. Biol. Chem. , vol.271 , pp. 6545-6554
    • Waegemann, K.1    Soll, J.2
  • 17
    • 33846029888 scopus 로고    scopus 로고
    • A protein kinase family in Arabidopsis phosphorylates chloroplast precursor proteins
    • Martin T., Sharma R., Sippel C., Waegemann K., Soll J., Vothknecht U.C. A protein kinase family in Arabidopsis phosphorylates chloroplast precursor proteins. J. Biol. Chem. 2006, 281:40216-40223.
    • (2006) J. Biol. Chem. , vol.281 , pp. 40216-40223
    • Martin, T.1    Sharma, R.2    Sippel, C.3    Waegemann, K.4    Soll, J.5    Vothknecht, U.C.6
  • 18
    • 33646593202 scopus 로고    scopus 로고
    • The molecular chaperone Hsp90 delivers precursor proteins to the chloroplast import receptor Toc64
    • Qbadou S., Becker T., Mirus O., Tews I., Soll J., Schleiff E. The molecular chaperone Hsp90 delivers precursor proteins to the chloroplast import receptor Toc64. EMBO J. 2006, 25:1836-1847.
    • (2006) EMBO J. , vol.25 , pp. 1836-1847
    • Qbadou, S.1    Becker, T.2    Mirus, O.3    Tews, I.4    Soll, J.5    Schleiff, E.6
  • 19
    • 0034712724 scopus 로고    scopus 로고
    • Toc34 is a preprotein receptor regulated by GTP and phosphorylation
    • Sveshnikova N., Soll J., Schleiff E. Toc34 is a preprotein receptor regulated by GTP and phosphorylation. PNAS 2000, 97:4973-4978.
    • (2000) PNAS , vol.97 , pp. 4973-4978
    • Sveshnikova, N.1    Soll, J.2    Schleiff, E.3
  • 20
    • 0027984260 scopus 로고
    • Identification of two GTP-binding proteins in the chloroplast protein import machinery
    • Kessler F., Blobel G., Patel H.A., Schnell D.J. Identification of two GTP-binding proteins in the chloroplast protein import machinery. Science 1994, 266:1035-1039.
    • (1994) Science , vol.266 , pp. 1035-1039
    • Kessler, F.1    Blobel, G.2    Patel, H.A.3    Schnell, D.J.4
  • 21
    • 0037065694 scopus 로고    scopus 로고
    • Structural and guanosine triphosphate/diphosphate requirements for transit peptide recognition by the cytosolic domain of the chloroplast outer envelope receptor, Toc34
    • Schleiff E., Soll J., Sveshnikova N., Tien R., Wright S., Dabney-Smith C., Subramanian C., Bruce B.D. Structural and guanosine triphosphate/diphosphate requirements for transit peptide recognition by the cytosolic domain of the chloroplast outer envelope receptor, Toc34. Biochemistry 2002, 41:1934-1946.
    • (2002) Biochemistry , vol.41 , pp. 1934-1946
    • Schleiff, E.1    Soll, J.2    Sveshnikova, N.3    Tien, R.4    Wright, S.5    Dabney-Smith, C.6    Subramanian, C.7    Bruce, B.D.8
  • 22
    • 0037447068 scopus 로고    scopus 로고
    • A GTP-driven motor moves proteins across the outer envelope of chloroplasts
    • Schleiff E., Jelic M., Soll J. A GTP-driven motor moves proteins across the outer envelope of chloroplasts. PNAS 2003, 100:4604-4660.
    • (2003) PNAS , vol.100 , pp. 4604-4660
    • Schleiff, E.1    Jelic, M.2    Soll, J.3
  • 23
    • 48649104944 scopus 로고    scopus 로고
    • Phosphorylation regulates the assembly of chloroplast import machinery
    • Oreb M., Höfle A., Mirus O., Schleiff E. Phosphorylation regulates the assembly of chloroplast import machinery. J. Exp. Bot. 2008, 59:2309-2316.
    • (2008) J. Exp. Bot. , vol.59 , pp. 2309-2316
    • Oreb, M.1    Höfle, A.2    Mirus, O.3    Schleiff, E.4
  • 24
    • 0034689055 scopus 로고    scopus 로고
    • Toc64, a new component of the protein translocon of chloroplasts
    • Sohrt K., Soll J. Toc64, a new component of the protein translocon of chloroplasts. J. Cell Biol. 2000, 148:1213-1221.
    • (2000) J. Cell Biol. , vol.148 , pp. 1213-1221
    • Sohrt, K.1    Soll, J.2
  • 25
    • 67649556148 scopus 로고    scopus 로고
    • Evolutionarily evolved discriminators in the 3-TPR domain of the Toc64 family involved in protein translocation at the outer membrane of chloroplasts and mitochondria
    • Mirus O., Bionda T., von Haeseler A., Schleiff E. Evolutionarily evolved discriminators in the 3-TPR domain of the Toc64 family involved in protein translocation at the outer membrane of chloroplasts and mitochondria. J. Mol. Model 2009, 15:971-982.
    • (2009) J. Mol. Model , vol.15 , pp. 971-982
    • Mirus, O.1    Bionda, T.2    von Haeseler, A.3    Schleiff, E.4
  • 26
    • 0344496513 scopus 로고    scopus 로고
    • The tetratricopeptide repeat: a structural motif mediating protein-protein interactions
    • Blatch G.L., Lässle M. The tetratricopeptide repeat: a structural motif mediating protein-protein interactions. BioEssays 1999, 21:932-939.
    • (1999) BioEssays , vol.21 , pp. 932-939
    • Blatch, G.L.1    Lässle, M.2
  • 27
    • 0035997027 scopus 로고    scopus 로고
    • The chloroplast protein import channel Toc75: pore properties and interaction with transit peptides
    • Hinnah S.C., Wagner R., Sveshnikova N., Harrer R., Soll J. The chloroplast protein import channel Toc75: pore properties and interaction with transit peptides. Biophys. J. 2002, 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
  • 29
    • 0033179289 scopus 로고    scopus 로고
    • The endosymbiotic origin of the protein import machinery of chloroplastic envelope membranes
    • Reumann S., Keegstra K. The endosymbiotic origin of the protein import machinery of chloroplastic envelope membranes. Trends Plant Sci. 1999, 4:302-307.
    • (1999) Trends Plant Sci. , vol.4 , pp. 302-307
    • Reumann, S.1    Keegstra, K.2
  • 30
    • 55549098175 scopus 로고    scopus 로고
    • The Omp85-related chloroplast outer envelope protein OEP80 is essential for viability in Arabidopsis
    • Patel R., Hsu S.-C., Bédard J., Inoue K., Jarvis P. The Omp85-related chloroplast outer envelope protein OEP80 is essential for viability in Arabidopsis. Plant Physiol. 2008, 148:235-245.
    • (2008) Plant Physiol. , vol.148 , pp. 235-245
    • Patel, R.1    Hsu, S.-C.2    Bédard, J.3    Inoue, K.4    Jarvis, P.5
  • 31
    • 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. Toc12, a novel subunit of the intermembrane space preprotein translocon of chloroplasts. Mol. Biol. Cell 2004, 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
  • 32
    • 0021100246 scopus 로고
    • Preparation and characterization of membrane fractions enriched in outer and inner envelope membranes from spinach chloroplasts. II. Biochemical characterization
    • Block M.A., Dorne A.J., Joyard J., Douce R. Preparation and characterization of membrane fractions enriched in outer and inner envelope membranes from spinach chloroplasts. II. Biochemical characterization. J. Biol. Chem. 1983, 258:13281-13286.
    • (1983) J. Biol. Chem. , vol.258 , pp. 13281-13286
    • Block, M.A.1    Dorne, A.J.2    Joyard, J.3    Douce, R.4
  • 33
    • 0028109712 scopus 로고
    • Isolation of components of the chloroplast protein import machinery
    • Schnell D.J., Kessler F., Blobel G. Isolation of components of the chloroplast protein import machinery. Science 1994, 266:1007-1012.
    • (1994) Science , vol.266 , pp. 1007-1012
    • Schnell, D.J.1    Kessler, F.2    Blobel, G.3
  • 34
    • 0029775088 scopus 로고    scopus 로고
    • Topology of IEP110, a component of the chloroplastic protein import machinery present in the inner envelope membrane
    • Lübeck J., Soll J., Akita M., Nielsen E., Keegstra K. Topology of IEP110, a component of the chloroplastic protein import machinery present in the inner envelope membrane. EMBO J. 1996, 15:4230-4238.
    • (1996) EMBO J. , vol.15 , pp. 4230-4238
    • Lübeck, J.1    Soll, J.2    Akita, M.3    Nielsen, E.4    Keegstra, K.5
  • 37
    • 0030997010 scopus 로고    scopus 로고
    • A nuclear-coded chloroplastic inner envelope membrane protein uses a soluble sorting intermediate upon import into the organelle
    • Lübeck J., Heins L., Soll J. A nuclear-coded chloroplastic inner envelope membrane protein uses a soluble sorting intermediate upon import into the organelle. J. Cell Biol. 1997, 137:1279-1286.
    • (1997) J. Cell Biol. , vol.137 , pp. 1279-1286
    • Lübeck, J.1    Heins, L.2    Soll, J.3
  • 38
    • 34249693697 scopus 로고    scopus 로고
    • Requirements for a conservative protein translocation pathway in chloroplasts
    • Vojta L., Soll J., Bölter B. Requirements for a conservative protein translocation pathway in chloroplasts. FEBS Lett. 2007, 581:2621-2624.
    • (2007) FEBS Lett. , vol.581 , pp. 2621-2624
    • Vojta, L.1    Soll, J.2    Bölter, B.3
  • 39
    • 0029798054 scopus 로고    scopus 로고
    • Interaction of the protein import and folding machineries of the chloroplast
    • Kessler F., Blobel G. Interaction of the protein import and folding machineries of the chloroplast. Proc. Natl. Acad. Sci. U. S. A. 1996, 93:7684-7689.
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 7684-7689
    • Kessler, F.1    Blobel, G.2
  • 40
    • 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 D.T., Froehlich J.E., Keegstra K. The hydrophilic domain of Tic110, an inner envelope membrane component of the chloroplastic protein translocation apparatus, faces the stromal compartment. J. Biol. Chem. 1998, 273:16583-16588.
    • (1998) J. Biol. Chem. , vol.273 , pp. 16583-16588
    • Jackson, D.T.1    Froehlich, J.E.2    Keegstra, K.3
  • 41
    • 0141866809 scopus 로고    scopus 로고
    • AtTic110 functions as a scaffold for coordinating the stromal events of protein import into chloroplasts
    • Inaba T., Li M., Alvarez-Huerta M., Kessler F., Schnell D.J. atTic110 functions as a scaffold for coordinating the stromal events of protein import into chloroplasts. J. Biol. Chem. 2003, 278:38617-38627.
    • (2003) J. Biol. Chem. , vol.278 , pp. 38617-38627
    • Inaba, T.1    Li, M.2    Alvarez-Huerta, M.3    Kessler, F.4    Schnell, D.J.5
  • 42
    • 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., Kessle F., Schnell D.J. Arabidopsis Tic110 is essential for the assembly and function of the protein import machinery of plastids. Plant Cell 2005, 17:1482-1496.
    • (2005) Plant Cell , vol.17 , pp. 1482-1496
    • Inaba, T.1    Alvarez-Huerta, M.2    Li, M.3    Bauer, J.4    Ewers, C.5    Kessle, F.6    Schnell, D.J.7
  • 43
    • 0033179289 scopus 로고    scopus 로고
    • The endosymbiotic origin of the protein import machinery of chloroplastic envelope membranes
    • Reumann S., Keegstra K. The endosymbiotic origin of the protein import machinery of chloroplastic envelope membranes. Trends Plant Sci. 1999, 4:302-307.
    • (1999) Trends Plant Sci. , vol.4 , pp. 302-307
    • Reumann, S.1    Keegstra, K.2
  • 44
    • 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
    • Kalanon M., McFadden G.I. The chloroplast protein translocation complexes of Chlamydomonas reinhardtii: a bioinformatic comparison of Toc and Tic components in plants, green algae and red algae. Genetics 2008, 179:95-112.
    • (2008) Genetics , vol.179 , pp. 95-112
    • Kalanon, M.1    McFadden, G.I.2
  • 45
    • 0037278304 scopus 로고    scopus 로고
    • Two chloroplastic protein translocation components, Tic110 and Toc75, are conserved in different plastid types from multiple plant species
    • Dávila-Aponte J.A., Inoue K., Keegstra K. Two chloroplastic protein translocation components, Tic110 and Toc75, are conserved in different plastid types from multiple plant species. Plant Mol. Biol. 2003, 51:175-181.
    • (2003) Plant Mol. Biol. , vol.51 , pp. 175-181
    • Dávila-Aponte, J.A.1    Inoue, K.2    Keegstra, K.3
  • 46
    • 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 D.J. Tic20 and Tic22 are new components of the protein import apparatus at the chloroplast inner envelope membrane. J. Cell Biol. 1998, 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
  • 47
    • 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 S.E., Schnell D.J. 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. J. Cell Biol. 1996, 134:315-327.
    • (1996) J. Cell Biol. , vol.134 , pp. 315-327
    • Ma, Y.1    Kouranov, A.2    LaSala, S.E.3    Schnell, D.J.4
  • 48
    • 0031408330 scopus 로고    scopus 로고
    • Analysis of the interactions of preproteins with the import machinery over the course of protein import into chloroplasts
    • Kouranov A., Schnell D.J. Analysis of the interactions of preproteins with the import machinery over the course of protein import into chloroplasts. J. Cell Biol. 1997, 139:1677-1685.
    • (1997) J. Cell Biol. , vol.139 , pp. 1677-1685
    • Kouranov, A.1    Schnell, D.J.2
  • 50
    • 0036009919 scopus 로고    scopus 로고
    • In vivo analysis of the role of atTic20 in protein import into chloroplasts
    • Chen X., Smith M.D., Fitzpatrick L., Schnell D.J. In vivo analysis of the role of atTic20 in protein import into chloroplasts. Plant Cell 2002, 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
  • 52
    • 70349229287 scopus 로고    scopus 로고
    • A 1-megadalton translocation complex containing Tic20 and Tic21 mediates chloroplast protein import at the inner envelope membrane
    • Kikuchi S., Oishi M., Hirabayashi Y., Lee D.W., Hwang I., Nakai M. A 1-megadalton translocation complex containing Tic20 and Tic21 mediates chloroplast protein import at the inner envelope membrane. Plant Cell 2009, 21:1781-1797.
    • (2009) Plant Cell , vol.21 , pp. 1781-1797
    • Kikuchi, S.1    Oishi, M.2    Hirabayashi, Y.3    Lee, D.W.4    Hwang, I.5    Nakai, M.6
  • 53
    • 33749242963 scopus 로고    scopus 로고
    • Tic21 is an essential translocon component for protein translocation across the chloroplast inner envelope membrane
    • Teng Y.S., Su Y.S., Chen L.J., Lee Y.J., Hwang I., Li H.M. Tic21 is an essential translocon component for protein translocation across the chloroplast inner envelope membrane. Plant Cell 2006, 18:2247-2257.
    • (2006) Plant Cell , vol.18 , pp. 2247-2257
    • Teng, Y.S.1    Su, Y.S.2    Chen, L.J.3    Lee, Y.J.4    Hwang, I.5    Li, H.M.6
  • 54
    • 34248146824 scopus 로고    scopus 로고
    • PIC1, an ancient permease in Arabidopsis chloroplasts, mediates iron transport
    • Duy D., Wanner G., Meda A.R., von Wiren N., Soll J., Philippar K. PIC1, an ancient permease in Arabidopsis chloroplasts, mediates iron transport. Plant Cell 2007, 19:986-1006.
    • (2007) Plant Cell , vol.19 , pp. 986-1006
    • Duy, D.1    Wanner, G.2    Meda, A.R.3    von Wiren, N.4    Soll, J.5    Philippar, K.6
  • 55
    • 67649198684 scopus 로고    scopus 로고
    • Translocons on the inner and outer envelopes of chloroplasts share similar evolutionary origin in Arabidopsis thaliana
    • Lv H.-X., Guo G.Q., Yang Z.-N. Translocons on the inner and outer envelopes of chloroplasts share similar evolutionary origin in Arabidopsis thaliana. J. Evol. Biol. 2009, 22:1418-1428.
    • (2009) J. Evol. Biol. , vol.22 , pp. 1418-1428
    • Lv, H.-X.1    Guo, G.Q.2    Yang, Z.-N.3
  • 56
    • 0023041137 scopus 로고
    • Energy dependence of protein translocation into chloroplasts
    • Flügge U.I., Hinz G. Energy dependence of protein translocation into chloroplasts. Eur. J. Biochem. 1986, 160:563-570.
    • (1986) Eur. J. Biochem. , vol.160 , pp. 563-570
    • Flügge, U.I.1    Hinz, G.2
  • 57
    • 0000079134 scopus 로고
    • Protein transport in chloroplasts: ATP is prerequisit
    • c
    • Schindler C., Hracky R., Soll J. Protein transport in chloroplasts: ATP is prerequisit. Z. Naturforsch 1987, 42c:103-108.
    • (1987) Z. Naturforsch , vol.42 , pp. 103-108
    • Schindler, C.1    Hracky, R.2    Soll, J.3
  • 58
    • 0030896924 scopus 로고    scopus 로고
    • Identification of protein transport complexes in the chloroplastic envelope membranes via chemical cross-linking
    • Akita M., Nielsen E., Keegstra K. Identification of protein transport complexes in the chloroplastic envelope membranes via chemical cross-linking. J. Cell Biol. 1997, 136:983-994.
    • (1997) J. Cell Biol. , vol.136 , pp. 983-994
    • Akita, M.1    Nielsen, E.2    Keegstra, K.3
  • 59
    • 0031048279 scopus 로고    scopus 로고
    • Stable association of chloroplastic precursors with protein translocation complexes that contain proteins from both envelope membranes and a stromal Hsp100 molecular chaperone
    • Nielsen E., Akita M., Dávila-Aponte J., Keegstra K. Stable association of chloroplastic precursors with protein translocation complexes that contain proteins from both envelope membranes and a stromal Hsp100 molecular chaperone. EMBO J. 1997, 16:935-946.
    • (1997) EMBO J. , vol.16 , pp. 935-946
    • Nielsen, E.1    Akita, M.2    Dávila-Aponte, J.3    Keegstra, K.4
  • 61
    • 0029392885 scopus 로고
    • The stroma of higher plant plastids contain ClpP and ClpC, functional homologs of Escherichia coli ClpP and ClpA: an archetypal two-component ATP-dependent protease
    • Shanklin J., DeWitt N.D., Flanagan J.M. The stroma of higher plant plastids contain ClpP and ClpC, functional homologs of Escherichia coli ClpP and ClpA: an archetypal two-component ATP-dependent protease. Plant Cell 1995, 7:1713-1722.
    • (1995) Plant Cell , vol.7 , pp. 1713-1722
    • Shanklin, J.1    DeWitt, N.D.2    Flanagan, J.M.3
  • 62
    • 0034850973 scopus 로고    scopus 로고
    • ATP-dependent association between subunits of Clp protease in pea chloroplasts
    • Halperin T., Ostersetzer O., Adam Z. ATP-dependent association between subunits of Clp protease in pea chloroplasts. Planta 2001, 213:614-619.
    • (2001) Planta , vol.213 , pp. 614-619
    • Halperin, T.1    Ostersetzer, O.2    Adam, Z.3
  • 63
    • 1042289735 scopus 로고    scopus 로고
    • Clp protease complexes from photosynthetic and non-photosynthetic plastids and mitochondria of plants, their predicted three-dimensional structures, and functional implications
    • Peltier J.B., Ripoll D.R., Friso G., Rudella A., Cai Y., Ytterberg J., Giacomelli L., Pillardy J., van Wijk K.J. Clp protease complexes from photosynthetic and non-photosynthetic plastids and mitochondria of plants, their predicted three-dimensional structures, and functional implications. J. Biol. Chem. 2004, 279:4768-4781.
    • (2004) J. Biol. Chem. , vol.279 , pp. 4768-4781
    • Peltier, J.B.1    Ripoll, D.R.2    Friso, G.3    Rudella, A.4    Cai, Y.5    Ytterberg, J.6    Giacomelli, L.7    Pillardy, J.8    van Wijk, K.J.9
  • 64
    • 34347232349 scopus 로고    scopus 로고
    • Distinctive types of ATP-dependent Clp proteases in Cyanobacteria
    • Stanne T.M., Pojidaeva E., Andersson F.I., Clarke A.K. Distinctive types of ATP-dependent Clp proteases in Cyanobacteria. J. Biol. Chem. 2007, 282:14394-14402.
    • (2007) J. Biol. Chem. , vol.282 , pp. 14394-14402
    • Stanne, T.M.1    Pojidaeva, E.2    Andersson, F.I.3    Clarke, A.K.4
  • 66
  • 67
    • 16544395791 scopus 로고    scopus 로고
    • A stromal Hsp100 protein is required for normal chloroplast development and function in Arabidopsis
    • Constan D., Froehlich J.E., Rangarajan S., Keegstra K. A stromal Hsp100 protein is required for normal chloroplast development and function in Arabidopsis. Plant Physiol. 2004, 136:3605-3615.
    • (2004) Plant Physiol. , vol.136 , pp. 3605-3615
    • Constan, D.1    Froehlich, J.E.2    Rangarajan, S.3    Keegstra, K.4
  • 68
    • 16644386554 scopus 로고    scopus 로고
    • Inactivation of the clpC1 gene encoding a chloroplast Hsp100 molecular chaperone causes growth retardation, leaf chlorosis, lower photosynthetic activity, and a specific reduction in photosystem content
    • Sjögren L.L.E., MacDonald T.M., Sutinen S., Clarke A.K. Inactivation of the clpC1 gene encoding a chloroplast Hsp100 molecular chaperone causes growth retardation, leaf chlorosis, lower photosynthetic activity, and a specific reduction in photosystem content. Plant Physiol. 2004, 136:4114-4126.
    • (2004) Plant Physiol. , vol.136 , pp. 4114-4126
    • Sjögren, L.L.E.1    MacDonald, T.M.2    Sutinen, S.3    Clarke, A.K.4
  • 69
    • 34247192598 scopus 로고    scopus 로고
    • Further in vivo studies on the role of the molecular chaperone, Hsp93, in plastid protein import
    • Kovacheva S., Bédard J., Wardle A., Patel R., Jarvis P. Further in vivo studies on the role of the molecular chaperone, Hsp93, in plastid protein import. Plant J. 2007, 50:364-379.
    • (2007) Plant J. , vol.50 , pp. 364-379
    • Kovacheva, S.1    Bédard, J.2    Wardle, A.3    Patel, R.4    Jarvis, P.5
  • 70
    • 33845712741 scopus 로고    scopus 로고
    • Stimulation of transit-peptide release and ATP hydrolysis by a cochaperone during protein import into chloroplasts
    • Chou M.L., Chu C.C., Chen L.J., Akita M., Li H.M. Stimulation of transit-peptide release and ATP hydrolysis by a cochaperone during protein import into chloroplasts. J. Cell Biol. 2006, 175:893-900.
    • (2006) J. Cell Biol. , vol.175 , pp. 893-900
    • Chou, M.L.1    Chu, C.C.2    Chen, L.J.3    Akita, M.4    Li, H.M.5
  • 71
    • 0033601180 scopus 로고    scopus 로고
    • Tic40, a new 'old' subunit of the chloroplast protein import translocon
    • Stahl T., Glockmann C., Soll J., Heins L. Tic40, a new 'old' subunit of the chloroplast protein import translocon. J. Biol. Chem. 1999, 274:37467-37472.
    • (1999) J. Biol. Chem. , vol.274 , pp. 37467-37472
    • Stahl, T.1    Glockmann, C.2    Soll, J.3    Heins, L.4
  • 72
    • 34547096291 scopus 로고    scopus 로고
    • Functional similarity between the chloroplast translocon component, Tic40, and the human co-chaperone, Hsp70-interacting protein (Hip)
    • Bédard J., Kubis S., Bimanadham S., Jarvis P. Functional similarity between the chloroplast translocon component, Tic40, and the human co-chaperone, Hsp70-interacting protein (Hip). J. Biol. Chem. 2007, 282:21404-21414.
    • (2007) J. Biol. Chem. , vol.282 , pp. 21404-21414
    • Bédard, J.1    Kubis, S.2    Bimanadham, S.3    Jarvis, P.4
  • 73
    • 57449097581 scopus 로고    scopus 로고
    • Tic40 is important for reinsertion of proteins from the chloroplast stroma into the inner membrane
    • Chiu C.C., Li H. Tic40 is important for reinsertion of proteins from the chloroplast stroma into the inner membrane. Plant J. 2008, 56:793-801.
    • (2008) Plant J. , vol.56 , pp. 793-801
    • Chiu, C.C.1    Li, H.2
  • 74
  • 75
    • 0037112789 scopus 로고    scopus 로고
    • Protein import into chloroplasts involves redox-regulated proteins
    • Küchler M., Decker S., Hörmann F., Soll J., Heins L. Protein import into chloroplasts involves redox-regulated proteins. EMBO J. 2002, 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
  • 76
    • 34047229926 scopus 로고    scopus 로고
    • Tic62: a protein family from metabolism to protein translocation
    • Balsera M., Stengel A., Soll J., Bölter B. Tic62: a protein family from metabolism to protein translocation. BMC Evol. Biol. 2007, 7:43.
    • (2007) BMC Evol. Biol. , vol.7 , pp. 43
    • Balsera, M.1    Stengel, A.2    Soll, J.3    Bölter, B.4
  • 77
    • 43749122140 scopus 로고    scopus 로고
    • TIC62 redox-regulated translocon composition and dynamics
    • Stengel A., Benz P., Balsera M., Soll J., Bölter B. TIC62 redox-regulated translocon composition and dynamics. J. Biol. Chem. 2008, 283:6656-6667.
    • (2008) J. Biol. Chem. , vol.283 , pp. 6656-6667
    • Stengel, A.1    Benz, P.2    Balsera, M.3    Soll, J.4    Bölter, B.5
  • 81
    • 4544377872 scopus 로고    scopus 로고
    • Tic32, an essential component in chloroplast biogenesis
    • correction, doi: 10.1074/jbc.A70786020010.1074/jbc.A402817200
    • Hörmann F., Küchler M., Sveshnikov D., Oppermann U., Li Y., Soll J. Tic32, an essential component in chloroplast biogenesis. J. Biol. Chem. 2004, 279:34756-34762. correction, doi: 10.1074/jbc.A70786020010.1074/jbc.A402817200.
    • (2004) J. Biol. Chem. , vol.279 , pp. 34756-34762
    • Hörmann, F.1    Küchler, M.2    Sveshnikov, D.3    Oppermann, U.4    Li, Y.5    Soll, J.6
  • 82
    • 0035028336 scopus 로고    scopus 로고
    • Maize non-photosynthetic ferredoxin precursor is mis-sorted to the intermembrane space of chloroplasts in the presence of light
    • Hirohashi T., Hase T., Nakai M. Maize non-photosynthetic ferredoxin precursor is mis-sorted to the intermembrane space of chloroplasts in the presence of light. Plant Physiol. 2001, 125:2154-2163.
    • (2001) Plant Physiol. , vol.125 , pp. 2154-2163
    • Hirohashi, T.1    Hase, T.2    Nakai, M.3
  • 83
    • 71249151181 scopus 로고    scopus 로고
    • Preprotein import into chloroplasts via the Toc and Tic complexes is regulated by redox signals in Pisum sativum
    • Stengel A., Benz J.P., Buchanan B.B., Soll J., Bölter B. Preprotein import into chloroplasts via the Toc and Tic complexes is regulated by redox signals in Pisum sativum. Molecular Plant 2009, 2:1181-1197.
    • (2009) Molecular Plant , vol.2 , pp. 1181-1197
    • Stengel, A.1    Benz, J.P.2    Buchanan, B.B.3    Soll, J.4    Bölter, B.5
  • 84
    • 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. The chloroplastic protein import machinery contains a Rieske-type iron-sulfur cluster and a mononuclear iron-binding protein. EMBO J. 1997, 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
  • 85
    • 3442885737 scopus 로고    scopus 로고
    • A small family of LLS1-related non-heme oxygenases in plants with an origin amongst oxygenic photosynthesizers
    • Gray J., Wardzala E., Yang M., Reinbothe S., Haller S., Pauli F. A small family of LLS1-related non-heme oxygenases in plants with an origin amongst oxygenic photosynthesizers. Plant Mol. Biol. 2004, 54:39-54.
    • (2004) Plant Mol. Biol. , vol.54 , pp. 39-54
    • Gray, J.1    Wardzala, E.2    Yang, M.3    Reinbothe, S.4    Haller, S.5    Pauli, F.6
  • 86
    • 71249085217 scopus 로고    scopus 로고
    • In vivo studies on the roles of Tic55-related proteins in chloroplast protein import in Arabidopsis thaliana
    • Boij P., Patel R., Garcia C., Jarvis P., Aronsson H. In vivo studies on the roles of Tic55-related proteins in chloroplast protein import in Arabidopsis thaliana. Molecular Plant 2009, 2:1397-1409.
    • (2009) Molecular Plant , vol.2 , pp. 1397-1409
    • Boij, P.1    Patel, R.2    Garcia, C.3    Jarvis, P.4    Aronsson, H.5
  • 87
    • 0031019820 scopus 로고    scopus 로고
    • Redox chains in chloroplast envelope membranes: spectroscopic evidence for the presence of electron carriers, including iron-sulfur centers
    • Jäger-Vottero P., Dorne A.J., Jordanov J., Douce R., Joyard J. Redox chains in chloroplast envelope membranes: spectroscopic evidence for the presence of electron carriers, including iron-sulfur centers. Proc. Natl. Acad. Sci. U. S. A. 1997, 94:1597-1602.
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 1597-1602
    • Jäger-Vottero, P.1    Dorne, A.J.2    Jordanov, J.3    Douce, R.4    Joyard, J.5
  • 88
    • 0032720826 scopus 로고    scopus 로고
    • An alternative electron transfer pathway mediated by chloroplast envelope
    • Murata Y., Takahashi M. An alternative electron transfer pathway mediated by chloroplast envelope. Plant Cell Physiol. 1999, 40:1007-1013.
    • (1999) Plant Cell Physiol. , vol.40 , pp. 1007-1013
    • Murata, Y.1    Takahashi, M.2
  • 90
    • 42949151399 scopus 로고    scopus 로고
    • The ferredoxin/thioredoxin system of oxygenic photosynthesis
    • Schürmann P., Buchanan B.B. The ferredoxin/thioredoxin system of oxygenic photosynthesis. Antioxid. Redox Signal. 2008, 10:1235-1274.
    • (2008) Antioxid. Redox Signal. , vol.10 , pp. 1235-1274
    • Schürmann, P.1    Buchanan, B.B.2
  • 92
    • 0142245708 scopus 로고    scopus 로고
    • Calcium/calmodulin-mediated signal network in plants
    • Yang T., Poovaiah B.W. Calcium/calmodulin-mediated signal network in plants. Trends Plant Sci. 2003, 8:505-512.
    • (2003) Trends Plant Sci. , vol.8 , pp. 505-512
    • Yang, T.1    Poovaiah, B.W.2
  • 93
    • 21244451176 scopus 로고    scopus 로고
    • Calcium regulation of chloroplast protein import
    • Chigri F., Soll J., Vothknecht U.C. Calcium regulation of chloroplast protein import. Plant J. 2005, 42:821-831.
    • (2005) Plant J. , vol.42 , pp. 821-831
    • Chigri, F.1    Soll, J.2    Vothknecht, U.C.3
  • 94
    • 0037155853 scopus 로고    scopus 로고
    • Genes encoding calmodulin-binding proteins in the Arabidopsis genome
    • Reddy V.S., Ali G.S., Reddy A.S.N. Genes encoding calmodulin-binding proteins in the Arabidopsis genome. J. Biol. Chem. 2002, 277:9840-9852.
    • (2002) J. Biol. Chem. , vol.277 , pp. 9840-9852
    • Reddy, V.S.1    Ali, G.S.2    Reddy, A.S.N.3
  • 95
    • 0036276574 scopus 로고    scopus 로고
    • Calmodulins and calcineurin B-like proteins: calcium sensors for specific signal response coupling in plants
    • Luan S., Kudla J., Rodriguez-Concepcion M., Yalovsky S., Gruissem W. Calmodulins and calcineurin B-like proteins: calcium sensors for specific signal response coupling in plants. Plant Cell 2002, 14:389-400.
    • (2002) Plant Cell , vol.14 , pp. 389-400
    • Luan, S.1    Kudla, J.2    Rodriguez-Concepcion, M.3    Yalovsky, S.4    Gruissem, W.5
  • 96
    • 66149192066 scopus 로고    scopus 로고
    • Calcium depletion and calmodulin inhibition affect the import of nuclear-encoded proteins into plant mitochondria
    • Kuhn S., Bussemer J., Chigri F., Vothknecht U.C. Calcium depletion and calmodulin inhibition affect the import of nuclear-encoded proteins into plant mitochondria. Plant J. 2009, 58:694-705.
    • (2009) Plant J. , vol.58 , pp. 694-705
    • Kuhn, S.1    Bussemer, J.2    Chigri, F.3    Vothknecht, U.C.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.