메뉴 건너뛰기




Volumn 75, Issue 5, 2013, Pages 847-857

Structural characterizations of the chloroplast translocon protein Tic110

Author keywords

chloroplast; CMQ 342 C; Cyanidioschyzon merolae; HEAT repeats; Tic110; translocon

Indexed keywords

CHLOROPLAST; CMQ 342 C; CYANIDIOSCHYZON MEROLAE; TIC110; TRANSLOCON;

EID: 84883209952     PISSN: 09607412     EISSN: 1365313X     Source Type: Journal    
DOI: 10.1111/tpj.12249     Document Type: Article
Times cited : (25)

References (51)
  • 1
    • 33749535905 scopus 로고    scopus 로고
    • Molecular architecture and assembly of the DDB1-CUL4A ubiquitin ligase machinery
    • Angers, S., Li, T., Yi, X., MacCoss, M.J., Moon, R.T., and, Zheng, N., (2006) Molecular architecture and assembly of the DDB1-CUL4A ubiquitin ligase machinery. Nature, 443, 590-593.
    • (2006) Nature , vol.443 , pp. 590-593
    • Angers, S.1    Li, T.2    Yi, X.3    MacCoss, M.J.4    Moon, R.T.5    Zheng, N.6
  • 3
    • 40749144066 scopus 로고    scopus 로고
    • De novo identification of highly diverged protein repeats by probabilistic consistency
    • Biegert, A., and, Soding, J., (2008) De novo identification of highly diverged protein repeats by probabilistic consistency. Bioinformatics, 24, 807-814.
    • (2008) Bioinformatics , vol.24 , pp. 807-814
    • Biegert, A.1    Soding, J.2
  • 4
    • 4243191428 scopus 로고
    • The fine structure of the chloroplast envelope of a red alga, Bangia fusco-purpurea
    • Bisalputra, T., and, Bailey, A., (1973) The fine structure of the chloroplast envelope of a red alga, Bangia fusco-purpurea. Protoplasma, 76, 443-454.
    • (1973) Protoplasma , vol.76 , pp. 443-454
    • Bisalputra, T.1    Bailey, A.2
  • 5
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography & NMR system: A new software suite for macromolecular structure determination
    • Brunger, A.T., Adams, P.D., Clore, G.M., et al. (1998) Crystallography & NMR system: a new software suite for macromolecular structure determination. Acta Crystallogr. D Biol. Crystallogr. 54, 905-921.
    • (1998) Acta Crystallogr. D Biol. Crystallogr. , vol.54 , pp. 905-921
    • Brunger, A.T.1    Adams, P.D.2    Clore, G.M.3
  • 8
    • 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., and, Li, H.m., (2006) Stimulation of transit-peptide release and ATP hydrolysis by a cochaperone during protein import into chloroplasts. J. Cell Biol. 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
  • 9
    • 84859340828 scopus 로고    scopus 로고
    • The N-terminal domain of chloroplast Hsp93 is important for its membrane association and functions in vivo
    • Chu, C.C., and, Li H.m., (2012) The N-terminal domain of chloroplast Hsp93 is important for its membrane association and functions in vivo. Plant Physiol. 158, 1656-1665.
    • (2012) Plant Physiol. , vol.158 , pp. 1656-1665
    • Chu, C.C.1    Li, H.-M.2
  • 10
    • 16544395791 scopus 로고    scopus 로고
    • A stromal Hsp100 protein is required for normal chloroplast development and function in Arabidopsis
    • Constan, D., Froehlich, J., Rangarajan, S., and, Keegstra, K., (2004) A stromal Hsp100 protein is required for normal chloroplast development and function in Arabidopsis. Plant Physiol. 136, 3605-3615.
    • (2004) Plant Physiol. , vol.136 , pp. 3605-3615
    • Constan, D.1    Froehlich, J.2    Rangarajan, S.3    Keegstra, K.4
  • 11
    • 0025224152 scopus 로고
    • Biochemistry and function of the plastid envelope
    • Douce, R., and, Joyard, J., (1990) Biochemistry and function of the plastid envelope. Annu. Rev. Cell Biol. 6, 173-216.
    • (1990) Annu. Rev. Cell Biol. , vol.6 , pp. 173-216
    • Douce, R.1    Joyard, J.2
  • 12
    • 0032935861 scopus 로고    scopus 로고
    • ChloroP, a neural network-based method for predicting chloroplast transit peptides and their cleavage sites
    • Emanuelsson, O., Nielsen, H., and, von Heijne, G., (1999) ChloroP, a neural network-based method for predicting chloroplast transit peptides and their cleavage sites. Protein Sci. 8, 978-984.
    • (1999) Protein Sci. , vol.8 , pp. 978-984
    • Emanuelsson, O.1    Nielsen, H.2    Von Heijne, G.3
  • 13
    • 0032961270 scopus 로고    scopus 로고
    • ESPript: Analysis of multiple sequence alignments in PostScript
    • Gouet, P., Courcelle, E., Stuart, D.I., and, Metoz, F., (1999) ESPript: analysis of multiple sequence alignments in PostScript. Bioinformatics, 15, 305-308.
    • (1999) Bioinformatics , vol.15 , pp. 305-308
    • Gouet, P.1    Courcelle, E.2    Stuart, D.I.3    Metoz, F.4
  • 14
    • 0000401603 scopus 로고
    • The chloroplast envelope - Structure, function, and role in leaf metabolism
    • Heber, U., and, Heldt, H.W., (1981) The chloroplast envelope-structure, function, and role in leaf metabolism. Annu. Rev. Plant. Biol. 32, 139-168.
    • (1981) Annu. Rev. Plant. Biol. , vol.32 , pp. 139-168
    • Heber, U.1    Heldt, H.W.2
  • 16
    • 0000207681 scopus 로고
    • TMBASE - A database of membrane spanning protein segments
    • Hofmann, K., and, Stoffel, W., (1993) TMBASE-A database of membrane spanning protein segments. Biol. Chem. Hoppe-Seyler, 374, 166.
    • (1993) Biol. Chem. Hoppe-Seyler , vol.374 , pp. 166
    • Hofmann, K.1    Stoffel, W.2
  • 17
    • 77954288774 scopus 로고    scopus 로고
    • Dali server: Conservation mapping in 3D
    • Holm, L., and, Rosenstrom, P., (2010) Dali server: conservation mapping in 3D. Nucleic Acids Res. 38, W545-W549.
    • (2010) Nucleic Acids Res. , vol.38
    • Holm, L.1    Rosenstrom, P.2
  • 18
    • 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., and, Schnell, D.J., (2003) atTic110 functions as a scaffold for coordinating the stromal events of protein import into chloroplasts. J. Biol. Chem. 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
  • 19
    • 30944465751 scopus 로고    scopus 로고
    • AtTic110 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., and, Schnell, D.J., (2005) atTic110 is essential for the assembly and function of the protein import machinery of plastids. Plant Cell, 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    Kessler, F.6    Schnell, D.J.7
  • 20
    • 84874281189 scopus 로고    scopus 로고
    • An essential role for chloroplast heat shock protein 90 (Hsp90C) in protein import into chloroplasts
    • Inoue, H., Li, M., and, Schnell, D.J., (2013) An essential role for chloroplast heat shock protein 90 (Hsp90C) in protein import into chloroplasts. Proc. Natl Acad. Sci. USA 110, 3173-3178.
    • (2013) Proc. Natl Acad. Sci. USA , vol.110 , pp. 3173-3178
    • Inoue, H.1    Li, M.2    Schnell, D.J.3
  • 21
    • 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., and, 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
  • 22
    • 47249152709 scopus 로고    scopus 로고
    • Targeting of nucleus-encoded proteins to chloroplasts in plants
    • Jarvis, P., (2008) Targeting of nucleus-encoded proteins to chloroplasts in plants. New Phytol. 179, 257-285.
    • (2008) New Phytol. , vol.179 , pp. 257-285
    • Jarvis, P.1
  • 23
    • 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., 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. Genetics, 179, 95-112.
    • (2008) Genetics , vol.179 , pp. 95-112
    • Kalanon, M.1    McFadden, G.I.2
  • 24
    • 63849246525 scopus 로고    scopus 로고
    • Protein structure prediction on the Web: A case study using the Phyre server
    • Kelley, L.A., and, Sternberg, M.J., (2009) Protein structure prediction on the Web: a case study using the Phyre server. Nat. Protoc. 4, 363-371.
    • (2009) Nat. Protoc. , vol.4 , pp. 363-371
    • Kelley, L.A.1    Sternberg, M.J.2
  • 25
    • 0029798054 scopus 로고    scopus 로고
    • Interaction of the protein import and folding machineries in the chloroplast
    • Kessler, F., and, Blobel, G., (1996) Interaction of the protein import and folding machineries in the chloroplast. Proc. Natl Acad. Sci. USA 93, 7684-7689.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 7684-7689
    • Kessler, F.1    Blobel, G.2
  • 26
    • 67949123338 scopus 로고    scopus 로고
    • Chloroplast biogenesis: Diversity and regulation of the protein import apparatus
    • Kessler, F., and, Schnell, D., (2009) Chloroplast biogenesis: diversity and regulation of the protein import apparatus. Curr. Opin. Cell Biol. 21, 494-500.
    • (2009) Curr. Opin. Cell Biol. , vol.21 , pp. 494-500
    • Kessler, F.1    Schnell, D.2
  • 27
    • 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., and, Nakai, M., (2009) A 1-megadalton translocation complex containing Tic20 and Tic21 mediates chloroplast protein import at the inner envelope membrane. Plant Cell, 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
  • 29
    • 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., and, Schnell, D.J., (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
  • 30
    • 13844261175 scopus 로고    scopus 로고
    • In vivo studies of the roles of Tic110, Tic40 and Hsp93 during chloroplast protein import
    • Kovacheva, S., Bedard, J., Patel, R., Dudley, P., Twell, D., Rios, G., Koncz, C., and, Jarvis, P., (2005) In vivo studies of the roles of Tic110, Tic40 and Hsp93 during chloroplast protein import. Plant J. 41, 412-428.
    • (2005) Plant J. , vol.41 , pp. 412-428
    • Kovacheva, S.1    Bedard, J.2    Patel, R.3    Dudley, P.4    Twell, D.5    Rios, G.6    Koncz, C.7    Jarvis, P.8
  • 31
    • 77953022036 scopus 로고    scopus 로고
    • Protein import into chloroplasts: The Tic complex and its regulation
    • Kovacs-Bogdan, E., Soll, J., and, Bolter, B., (2010) Protein import into chloroplasts: the Tic complex and its regulation. Biochim. Biophys. Acta, 1803, 740-747.
    • (2010) Biochim. Biophys. Acta , vol.1803 , pp. 740-747
    • Kovacs-Bogdan, E.1    Soll, J.2    Bolter, B.3
  • 32
    • 80053345339 scopus 로고    scopus 로고
    • Tic20 forms a channel independent of Tic110 in chloroplasts
    • Kovacs-Bogdan, E., Benz, J.P., Soll, J., and, Bolter, B., (2011) Tic20 forms a channel independent of Tic110 in chloroplasts. BMC Plant Biol., 11, 133.
    • (2011) BMC Plant Biol. , vol.11 , pp. 133
    • Kovacs-Bogdan, E.1    Benz, J.P.2    Soll, J.3    Bolter, B.4
  • 33
    • 77952506871 scopus 로고    scopus 로고
    • Protein transport into chloroplasts
    • Li H.m., and, Chiu C.C., (2010) Protein transport into chloroplasts. Annu. Rev. Plant Biol. 61, 157-180.
    • (2010) Annu. Rev. Plant Biol. , vol.61 , pp. 157-180
    • Li, H.M.1    Chiu, C.C.2
  • 34
    • 57849093142 scopus 로고    scopus 로고
    • A dedicated small-angle X-ray scattering beamline with a superconducting wiggler source at the NSRRC
    • Liu, D.G., Chang, C.H., Liu, C.Y., et al. (2009) A dedicated small-angle X-ray scattering beamline with a superconducting wiggler source at the NSRRC. J. Synchrotron Radiat. 16, 97-104.
    • (2009) J. Synchrotron Radiat. , vol.16 , pp. 97-104
    • Liu, D.G.1    Chang, C.H.2    Liu, C.Y.3
  • 35
    • 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., and, Soll, J., (1997) A nuclear-coded chloroplastic inner envelope membrane protein uses a soluble sorting intermediate upon import into the organelle. J. Cell Biol. 137, 1279-1286.
    • (1997) J. Cell Biol. , vol.137 , pp. 1279-1286
    • Lübeck, J.1    Heins, L.2    Soll, J.3
  • 36
    • 11144354393 scopus 로고    scopus 로고
    • Genome sequence of the ultrasmall unicellular red alga Cyanidioschyzon merolae 10D
    • Matsuzaki, M., Misumi, O., Shin, I.T., et al. (2004) Genome sequence of the ultrasmall unicellular red alga Cyanidioschyzon merolae 10D. Nature, 428, 653-657.
    • (2004) Nature , vol.428 , pp. 653-657
    • Matsuzaki, M.1    Misumi, O.2    Shin, I.T.3
  • 37
    • 0025272639 scopus 로고
    • Current approaches to macromolecular crystallization
    • McPherson, A., (1990) Current approaches to macromolecular crystallization. Eur. J. Biochem. 189, 1-23.
    • (1990) Eur. J. Biochem. , vol.189 , pp. 1-23
    • McPherson, A.1
  • 38
    • 0032790081 scopus 로고    scopus 로고
    • XtalView/Xfit-A versatile program for manipulating atomic coordinates and electron density
    • McRee, D.E., (1999) XtalView/Xfit-A versatile program for manipulating atomic coordinates and electron density. J. Struct. Biol. 125, 156-165.
    • (1999) J. Struct. Biol. , vol.125 , pp. 156-165
    • McRee, D.E.1
  • 39
    • 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., Davila-Aponte, J., and, Keegstra, K., (1997) Stable association of chloroplastic precursors with protein translocation complexes that contain proteins from both envelope membranes and a stromal Hsp100 molecular chaperone. EMBO J. 16, 935-946.
    • (1997) EMBO J. , vol.16 , pp. 935-946
    • Nielsen, E.1    Akita, M.2    Davila-Aponte, J.3    Keegstra, K.4
  • 40
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z., and, Minor, W., (1997) Processing of X-ray diffraction data collected in oscillation mode. Meth. Enzymol. 276, 307-326.
    • (1997) Meth. Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 41
    • 0025987220 scopus 로고
    • In vitro reconstitution of protein transport into chloroplasts
    • Perry, S.E., Li H.-m., and, Keegstra K., (1991) In vitro reconstitution of protein transport into chloroplasts. Methods Cell Biol. 34, 327-344.
    • (1991) Methods Cell Biol. , vol.34 , pp. 327-344
    • Perry, S.E.1    Li, H.-M.2    Keegstra, K.3
  • 42
    • 34248359067 scopus 로고    scopus 로고
    • ATSAS 2.1 - Towards automated and web-supported small-angle scattering data analysis
    • Petoukhov, M.V., Konarev, P.V., Kikhney, A.G., and, Svergun, D.I., (2007) ATSAS 2.1-towards automated and web-supported small-angle scattering data analysis. J. Appl. Crystallogr. 40, s223-s228.
    • (2007) J. Appl. Crystallogr. , vol.40
    • Petoukhov, M.V.1    Konarev, P.V.2    Kikhney, A.G.3    Svergun, D.I.4
  • 43
    • 77950347530 scopus 로고    scopus 로고
    • A stromal heat shock protein 70 system functions in protein import into chloroplasts in the moss Physcomitrella patens
    • Shi, L.X., and, Theg, S.M., (2010) A stromal heat shock protein 70 system functions in protein import into chloroplasts in the moss Physcomitrella patens. Plant Cell, 22, 205-220.
    • (2010) Plant Cell , vol.22 , pp. 205-220
    • Shi, L.X.1    Theg, S.M.2
  • 44
    • 84871749722 scopus 로고    scopus 로고
    • The chloroplast protein import system: From algae to trees
    • Shi, L.X., and, Theg, S.M., (2013) The chloroplast protein import system: from algae to trees. Biochim. Biophys. Acta, 1833, 314-331.
    • (2013) Biochim. Biophys. Acta , vol.1833 , pp. 314-331
    • Shi, L.X.1    Theg, S.M.2
  • 45
    • 77954410967 scopus 로고    scopus 로고
    • Stromal Hsp70 is important for protein translocation into pea and Arabidopsis chloroplasts
    • Su, P.H., and, Li H.m., (2010) Stromal Hsp70 is important for protein translocation into pea and Arabidopsis chloroplasts. Plant Cell, 22, 1516-1531.
    • (2010) Plant Cell , vol.22 , pp. 1516-1531
    • Su, P.H.1    Li, H.M.2
  • 46
    • 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., and, Li, H.m., (2006) Tic21 is an essential translocon component for protein translocation across the chloroplast inner envelope membrane. Plant Cell, 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
  • 50
    • 69849086706 scopus 로고    scopus 로고
    • Architectural nucleoporins Nup157/170 and Nup133 are structurally related and descend from a second ancestral element
    • Whittle, J.R., and, Schwartz, T.U., (2009) Architectural nucleoporins Nup157/170 and Nup133 are structurally related and descend from a second ancestral element. J. Biol. Chem. 284, 28442-28452.
    • (2009) J. Biol. Chem. , vol.284 , pp. 28442-28452
    • Whittle, J.R.1    Schwartz, T.U.2
  • 51
    • 18344391432 scopus 로고    scopus 로고
    • Structure of the Cul1-Rbx1-Skp1-F boxSkp2 SCF ubiquitin ligase complex
    • Zheng, N., Schulman, B.A., Song, L., et al. (2002) Structure of the Cul1-Rbx1-Skp1-F boxSkp2 SCF ubiquitin ligase complex. Nature, 416, 703-709.
    • (2002) Nature , vol.416 , pp. 703-709
    • Zheng, N.1    Schulman, B.A.2    Song, L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.