메뉴 건너뛰기




Volumn 6, Issue 3, 2013, Pages 817-829

In vivo function of Tic22, a protein import component of the intermembrane space of chloroplasts

Author keywords

chloroplast biogenesis; intermembrane space translocon; metabolite content; protein translocation; TOC and TIC

Indexed keywords

ARABIDOPSIS THALIANA;

EID: 84878315892     PISSN: 16742052     EISSN: 17529867     Source Type: Journal    
DOI: 10.1093/mp/sss114     Document Type: Article
Times cited : (31)

References (63)
  • 1
    • 0030896924 scopus 로고    scopus 로고
    • Identification of protein transport complexes in the chloroplastic envelope membranes via chemical cross-linking
    • Akita, M., Nielsen, E., and Keegstra, K. (1997). Identification of protein transport complexes in the chloroplastic envelope membranes via chemical cross-linking. J. Cell Biol. 136, 983-994.
    • (1997) J. Cell Biol , vol.136 , pp. 983-994
    • Akita, M.1    Nielsen, E.2    Keegstra, K.3
  • 2
    • 77954395693 scopus 로고    scopus 로고
    • Identification of the 2-hydroxyglutarate and isovaleryl- CoA dehydrogenases as alternative electron donors linking lysine catabolism to the electron transport chain of Arabidopsis mitochondria
    • Araújo, W.L., Ishizaki, K., Nunes-Nesi, A., Larson, T.R., Tohge, T., Krahnert, I., Witt, S., Obata, T., Schauer, N., Graham, I.A., et al. (2010). Identification of the 2-hydroxyglutarate and isovaleryl- CoA dehydrogenases as alternative electron donors linking lysine catabolism to the electron transport chain of Arabidopsis mitochondria. Plant Cell. 22, 1549-1563.
    • (2010) Plant Cell. , vol.22 , pp. 1549-1563
    • Araújo, W.L.1    Ishizaki, K.2    Nunes-Nesi, A.3    Larson, T.R.4    Tohge, T.5    Krahnert, I.6    Witt, S.7    Obata, T.8    Schauer, N.9    Graham, I.A.10
  • 3
    • 0001844190 scopus 로고
    • Copper enzymes in isolated chloroplasts: Polyphenoloxidase in Beta vulgaris
    • Arnon, D. (1949). Copper enzymes in isolated chloroplasts: polyphenoloxidase in Beta vulgaris. Plant Physiol. 24, 1-15.
    • (1949) Plant Physiol , vol.24 , pp. 1-15
    • Arnon, D.1
  • 4
    • 0037048707 scopus 로고    scopus 로고
    • A simple method for isolating import-competent Arabidopsis chloroplasts
    • Aronsson, H., and Jarvis, P. (2002). A simple method for isolating import-competent Arabidopsis chloroplasts. FEBS Lett. 529, 215-220.
    • (2002) FEBS Lett , vol.529 , pp. 215-220
    • Aronsson, H.1    Jarvis, P.2
  • 5
    • 80052930070 scopus 로고    scopus 로고
    • Rapid isolation of Arabidopsis chloroplasts and their use for in vitro protein import assays
    • Jarvis, R.P., ed. (Totowa, NJ: Humana Press)
    • Aronsson, H., and Jarvis, R.P. (2011). Rapid isolation of Arabidopsis chloroplasts and their use for in vitro protein import assays. In Chloroplast Research in Arabidopsis: Methods and Protocols, Volume 1. Jarvis, R.P., ed. (Totowa, NJ: Humana Press), pp. 281-305.
    • (2011) Chloroplast Research in Arabidopsis: Methods and Protocols , vol.1 , pp. 281-305
    • Aronsson, H.1    Jarvis, R.P.2
  • 6
    • 34748865489 scopus 로고    scopus 로고
    • Toc64/OEP64 is not essential for the efficient import of proteins into chloroplasts in Arabidopsis thaliana
    • Aronsson, H., Boij, P., Patel, R., Wardle, A., Töpel, M., and Jarvis, P. (2007). Toc64/OEP64 is not essential for the efficient import of proteins into chloroplasts in Arabidopsis thaliana. Plant J. 52, 53-68.
    • (2007) Plant J , vol.52 , pp. 53-68
    • Aronsson, H.1    Boij, P.2    Patel, R.3    Wardle, A.4    Töpel, M.5    Jarvis, P.6
  • 7
    • 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., and 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
  • 8
    • 77956913411 scopus 로고    scopus 로고
    • Chloroplast import signals: The length requirement for translocation in vitro and in vivo
    • Bionda, T., Tillmann, B., Simm, S., Beilstein, K., Ruprecht, M., and Schleiff, E. (2010). Chloroplast import signals: the length requirement for translocation in vitro and in vivo. J. Mol. Biol. 402, 510-523.
    • (2010) J. Mol. Biol. , vol.402 , pp. 510-523
    • Bionda, T.1    Tillmann, B.2    Simm, S.3    Beilstein, K.4    Ruprecht, M.5    Schleiff, E.6
  • 9
    • 57049142069 scopus 로고    scopus 로고
    • Quantitative analysis of snoRNA association with pre-ribosomes and release of snR30 by Rok1 helicase
    • Bohnsack, M.T., Kos, M., and Tollervey, D. (2008). Quantitative analysis of snoRNA association with pre-ribosomes and release of snR30 by Rok1 helicase. EMBO Rep. 9, 1230-1236.
    • (2008) EMBO Rep , vol.9 , pp. 1230-1236
    • Bohnsack, M.T.1    Kos, M.2    Tollervey, D.3
  • 10
    • 0034928217 scopus 로고    scopus 로고
    • Growth stage-based phenotypic analysis of Arabidopsis: A model for high throughput functional genomics in plants
    • Boyes, D.C., Zayed, A.M., Ascenzi, R., McCaskill, A.J., Hoffman, N.E., Davis, K.R., and Gorlach, J. (2001). Growth stage-based phenotypic analysis of Arabidopsis: a model for high throughput functional genomics in plants. Plant Cell. 13, 1499-1510.
    • (2001) Plant Cell , vol.13 , pp. 1499-1510
    • Boyes, D.C.1    Zayed, A.M.2    Ascenzi, R.3    McCaskill, A.J.4    Hoffman, N.E.5    Davis, K.R.6    Gorlach, J.7
  • 11
    • 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., and Schnell, D.J. (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
  • 12
    • 78249244763 scopus 로고    scopus 로고
    • Pea chloroplast DnaJ-J8 and Toc12 are encoded by the same gene and localized in the stroma
    • Chiu, C.C., Chen, L.J., and Li, H.M. (2010). Pea chloroplast DnaJ-J8 and Toc12 are encoded by the same gene and localized in the stroma. Plant Physiol. 154, 1172-1182.
    • (2010) Plant Physiol. , vol.154 , pp. 1172-1182
    • Chiu, C.C.1    Chen, L.J.2    Li, H.M.3
  • 13
    • 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
  • 15
    • 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., 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.E.2    Rangarajan, S.3    Keegstra, K.4
  • 16
    • 80052418295 scopus 로고    scopus 로고
    • Cytosolic HSP90 cochaperones HOP and FKBP interact with freshly synthesized chloroplast preproteins of Arabidopsis
    • Fellerer, C., Schweiger, R., Schöngruber, K., Soll, J., and Schwenkert, S. (2011). Cytosolic HSP90 cochaperones HOP and FKBP interact with freshly synthesized chloroplast preproteins of Arabidopsis. Mol. Plant. 4, 1133-1145.
    • (2011) Mol. Plant. , vol.4 , pp. 1133-1145
    • Fellerer, C.1    Schweiger, R.2    Schöngruber, K.3    Soll, J.4    Schwenkert, S.5
  • 17
    • 84862170465 scopus 로고    scopus 로고
    • Validated high quality automated metabolome analysis of Arabidopsis thaliana leaf discs: Quality control charts and standard operating procedures
    • Nikolau, B.J., and Wurtele, E.S., eds (Dordrecht, The Netherlands: Springer)
    • Fiehn, O. (2007). Validated high quality automated metabolome analysis of Arabidopsis thaliana leaf discs: quality control charts and standard operating procedures. In Concepts in Plant Metabolomics, Nikolau, B.J., and Wurtele, E.S., eds (Dordrecht, The Netherlands: Springer), pp. 1-18.
    • (2007) Concepts in Plant Metabolomics , pp. 1-18
    • Fiehn, O.1
  • 18
    • 0033802314 scopus 로고    scopus 로고
    • Functional analysis of the two Arabidopsis homologues of Toc34, a component of the chloroplast protein import apparatus
    • Gutensohn, M., Schulz, B., Nicolay, P., and Flügge, 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.
    • (2000) Plant J , vol.23 , pp. 771-783
    • Gutensohn, M.1    Schulz, B.2    Nicolay, P.3    Flügge, U.I.4
  • 19
    • 0028857259 scopus 로고
    • The shikimate pathway: Early steps in the biosynthesis of aromatic compounds
    • Herrmann, K.M. (1995). The shikimate pathway: early steps in the biosynthesis of aromatic compounds. Plant Cell. 7, 907-919.
    • (1995) Plant Cell , vol.7 , pp. 907-919
    • Herrmann, K.M.1
  • 20
    • 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
  • 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
    • 0035037171 scopus 로고    scopus 로고
    • Arabidopsis genes encoding components of the chloroplastic protein import apparatus
    • Jackson-Constan, D., and 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
  • 23
    • 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
  • 24
    • 0032476027 scopus 로고    scopus 로고
    • An Arabidopsis mutant defective in the plastid general protein import apparatus
    • 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.
    • (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
  • 25
    • 68549083618 scopus 로고    scopus 로고
    • Characterization of two putative protein translocation components in the apicoplast of Plasmodium falciparum
    • Kalanon, M., Tonkin, C.J., and McFadden, G.I. (2009). Characterization of two putative protein translocation components in the apicoplast of Plasmodium falciparum. Eukaryot. Cell. 8, 1146-1154.
    • (2009) Eukaryot. Cell , vol.8 , pp. 1146-1154
    • Kalanon, M.1    Tonkin, C.J.2    McFadden, G.I.3
  • 26
    • 79957602399 scopus 로고    scopus 로고
    • Molecular and genetic analyses of Tic20 homologues in Arabidopsis thaliana chloroplasts
    • Kasmati, A.R., Töpel, M., Patel, R., Murtaza, G., and Jarvis, P. (2011). Molecular and genetic analyses of Tic20 homologues in Arabidopsis thaliana chloroplasts. Plant J. 66, 877-889.
    • (2011) Plant J. , vol.66 , pp. 877-889
    • Kasmati, A.R.1    Töpel, M.2    Patel, R.3    Murtaza, G.4    Jarvis, P.5
  • 27
    • 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
  • 28
    • 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., 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.
    • (1997) J. Cell Biol , vol.139 , pp. 1677-1685
    • Kouranov, A.1    Schnell, D.J.2
  • 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
    • 0033609884 scopus 로고    scopus 로고
    • Tic22 is targeted to the intermembrane space of chloroplasts by a novel pathway
    • Kouranov, A., Wang, H., and Schnell, D.J. (1999). Tic22 is targeted to the intermembrane space of chloroplasts by a novel pathway. J. Biol. Chem. 274, 25181-25186.
    • (1999) J. Biol. Chem , vol.274 , pp. 25181-25186
    • Kouranov, A.1    Wang, H.2    Schnell, D.J.3
  • 31
    • 13844261175 scopus 로고    scopus 로고
    • In vivo studies on the roles of Tic110, Tic40 and Hsp93 during chloroplast protein import
    • Kovacheva, S., Bedard, J., Patel, R., Dudley, P., Twell, D., and Rios, G. (2005). In vivo studies on 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
  • 32
    • 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., and Jarvis, P. (2007). Further in vivo studies on the role of the molecular chaperone, Hsp93, in plastid protein import. Plant J. 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
  • 33
    • 80053345339 scopus 로고    scopus 로고
    • Tic20 forms a channel independent of Tic110 in chloroplasts
    • Kovács-Bogdán, E., Benz, J.P., Soll, J., and Bölter, B. (2011). Tic20 forms a channel independent of Tic110 in chloroplasts. BMC Plant Biol. 11, 133.
    • (2011) BMC Plant Biol. , vol.11 , pp. 133
    • Kovács-Bogdán, E.1    Benz, J.P.2    Soll, J.3    Bölter, B.4
  • 34
    • 0041920588 scopus 로고    scopus 로고
    • The Arabidopsis ppi1 mutant is specifically defective in the expression, chloroplast import, and accumulation of photosynthetic proteins
    • Kubis, S., Baldwin, A., Patel, R., Razzaq, A., Dupree, P., Lilley, K., Kurth, J., Leister, D., and Jarvis, P. (2003). The Arabidopsis ppi1 mutant is specifically defective in the expression, chloroplast import, and accumulation of photosynthetic proteins. Plant Cell. 15, 1859-1871.
    • (2003) Plant Cell , vol.15 , pp. 1859-1871
    • Kubis, S.1    Baldwin, A.2    Patel, R.3    Razzaq, A.4    Dupree, P.5    Lilley, K.6    Kurth, J.7    Leister, D.8    Jarvis, P.9
  • 36
    • 43649098283 scopus 로고    scopus 로고
    • High quality metabolomic data for Chlamydomonas reinhardtii
    • Lee, D.Y., and Fiehn, O. (2008). High quality metabolomic data for Chlamydomonas reinhardtii. Plant Methods. 4, 7.
    • (2008) Plant Methods , vol.4 , pp. 7
    • Lee, D.Y.1    Fiehn, O.2
  • 37
    • 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
  • 38
    • 80054026313 scopus 로고    scopus 로고
    • The localization of Tic20 proteins in Arabidopsis thaliana is not restricted to the inner envelope membrane of chloroplasts
    • Machettira, A.B., Gross, L.E., Sommer, M.S., Weis, B.L., Englich, G., Tripp, J., and Schleiff, E. (2011). The localization of Tic20 proteins in Arabidopsis thaliana is not restricted to the inner envelope membrane of chloroplasts. Plant Mol. Biol. 77, 381-390.
    • (2011) Plant Mol. Biol. , vol.77 , pp. 381-390
    • MacHettira, A.B.1    Gross, L.E.2    Sommer, M.S.3    Weis, B.L.4    Englich, G.5    Tripp, J.6    Schleiff, E.7
  • 40
    • 0033950443 scopus 로고    scopus 로고
    • 14-3-3 proteins form a guidance complex with chloroplast precursor proteins in plants
    • May, T., and Soll, J. (2000). 14-3-3 proteins form a guidance complex with chloroplast precursor proteins in plants. Plant Cell. 12, 53-64.
    • (2000) Plant Cell , vol.12 , pp. 53-64
    • May, T.1    Soll, J.2
  • 41
    • 18844455516 scopus 로고    scopus 로고
    • Analysis of expression patterns of translocon subunits of chloroplasts and mitochondria
    • Moghadam, M.A.K., and Schleiff, E. (2005). Analysis of expression patterns of translocon subunits of chloroplasts and mitochondria. Plant Science. 68, 1533-1539.
    • (2005) Plant Science , vol.68 , pp. 1533-1539
    • Moghadam, M.A.K.1    Schleiff, E.2
  • 42
    • 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
  • 43
    • 37049034073 scopus 로고    scopus 로고
    • Phospho-mimicry mutant of atToc33 affects early development of Arabidopsis thaliana
    • Oreb, M., Zoryan, M., Vojta, A., Maier, U.G., Eichacker, L.A., and Schleiff, E. (2007). Phospho-mimicry mutant of atToc33 affects early development of Arabidopsis thaliana. FEBS Lett. 581, 5945-5951.
    • (2007) FEBS Lett , vol.581 , pp. 5945-5951
    • Oreb, M.1    Zoryan, M.2    Vojta, A.3    Maier, U.G.4    Eichacker, L.A.5    Schleiff, E.6
  • 44
  • 45
    • 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., and Schleiff, E. (2006). The molecular chaperone Hsp90 delivers precursor proteins to the chloroplast import receptor Toc64. EMBO J. 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
  • 46
    • 30944433280 scopus 로고    scopus 로고
    • Toc64 is not required for import of proteins into chloroplasts in the moss Physcomitrella patens
    • Rosenbaum-Hofmann, N., and Theg, S.M. (2005). Toc64 is not required for import of proteins into chloroplasts in the moss Physcomitrella patens. Plant J. 43, 675-687.
    • (2005) Plant J , vol.43 , pp. 675-687
    • Rosenbaum-Hofmann, N.1    Theg, S.M.2
  • 47
    • 1642465435 scopus 로고    scopus 로고
    • An Arabidopsis thaliana T-DNA mutagenized population (GABI-kat) for flanking sequence tag-based reverse genetics
    • Rosso M.G., Li Y., Strizhov N., Reiss B., Dekker K., and Weisshaar B. (2003) An Arabidopsis thaliana T-DNA mutagenized population (GABI-kat) for flanking sequence tag-based reverse genetics. Plant Mol. Biol. 53, 247-259.
    • (2003) Plant Mol. Biol , vol.53 , pp. 247-259
    • Rosso, M.G.1    Li, Y.2    Strizhov, N.3    Reiss, B.4    Dekker, K.5    Weisshaar, B.6
  • 48
    • 77952983547 scopus 로고    scopus 로고
    • On the impact of precursor unfolding during protein import into chloroplasts
    • Ruprecht, M., Bionda, T., Sato, T., Sommer, M.S., Endo, T., and Schleiff, E. (2010). On the impact of precursor unfolding during protein import into chloroplasts. Mol. Plant. 3, 499-508.
    • (2010) Mol. Plant. , vol.3 , pp. 499-508
    • Ruprecht, M.1    Bionda, T.2    Sato, T.3    Sommer, M.S.4    Endo, T.5    Schleiff, E.6
  • 49
    • 78650517733 scopus 로고    scopus 로고
    • Common ground for protein translocation: Access control for mitochondria and chloroplasts
    • Schleiff, E., and Becker, T. (2011). Common ground for protein translocation: access control for mitochondria and chloroplasts. Nat. Rev. Mol. Cell Biol. 12, 48-59.
    • (2011) Nat. Rev. Mol. Cell Biol. , vol.12 , pp. 48-59
    • Schleiff, E.1    Becker, T.2
  • 50
    • 0028109712 scopus 로고
    • Isolation of components of the chloroplast protein import machinery
    • Schnell, D.J., Kessler, F., and Blobel, G. (1994). Isolation of components of the chloroplast protein import machinery. Science. 266, 1007-1012.
    • (1994) Science , vol.266 , pp. 1007-1012
    • Schnell, D.J.1    Kessler, F.2    Blobel, G.3
  • 52
    • 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
  • 53
    • 1542374116 scopus 로고    scopus 로고
    • Protein import into chloroplasts
    • Soll, J., and Schleiff, E. (2004). Protein import into chloroplasts. Nat. Rev. Mol. Cell Biol. 5, 198-208.
    • (2004) Nat. Rev. Mol. Cell Biol , vol.5 , pp. 198-208
    • Soll, J.1    Schleiff, E.2
  • 54
    • 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
  • 55
    • 64849088674 scopus 로고    scopus 로고
    • A protocol for efficiently retrieving and characterizing flanking sequence tags (FSTs) in Brachypodium distachyon T-DNA insertional mutants
    • Thole, V., Alves, S.C., Worland, B., Bevan, M.W., and Vain, P. (2009). A protocol for efficiently retrieving and characterizing flanking sequence tags (FSTs) in Brachypodium distachyon T-DNA insertional mutants. Nat. Protoc. 4, 650-661.
    • (2009) Nat. Protoc , vol.4 , pp. 650-661
    • Thole, V.1    Alves, S.C.2    Worland, B.3    Bevan, M.W.4    Vain, P.5
  • 56
    • 0027536925 scopus 로고
    • Interaction of homologues of Hsp70 and Cpn60 with ferredoxin-NADP+ reductase upon its import into chloroplasts
    • Tsugeki, R., and Nishimura, M. (1993). Interaction of homologues of Hsp70 and Cpn60 with ferredoxin-NADP+ reductase upon its import into chloroplasts. FEBS Lett. 320, 198-202.
    • (1993) FEBS Lett , vol.320 , pp. 198-202
    • Tsugeki, R.1    Nishimura, M.2
  • 57
    • 84865025618 scopus 로고    scopus 로고
    • Chloroplast β-barrel proteins are assembled into the mitochondrial outer membrane in a process that depends on the TOM and TOB complexes
    • Ulrich, T., Gross, L.E., Sommer M.S., Schleiff, E., and Rapaport, D. (2012). Chloroplast β-barrel proteins are assembled into the mitochondrial outer membrane in a process that depends on the TOM and TOB complexes. J. Biol. Chem. 287, 27467-27479.
    • (2012) J. Biol. Chem. , vol.287 , pp. 27467-27479
    • Ulrich, T.1    Gross, L.E.2    Sommer, M.S.3    Schleiff, E.4    Rapaport, D.5
  • 59
    • 34748905237 scopus 로고    scopus 로고
    • Protein transport in chloroplasts: Targeting to the intermembrane space
    • Vojta, L., Soll, J., and Bölter, B. (2007). Protein transport in chloroplasts: targeting to the intermembrane space. FEBS J. 274, 5043-5054.
    • (2007) FEBS J , vol.274 , pp. 5043-5054
    • Vojta, L.1    Soll, J.2    Bölter, B.3
  • 60
    • 0000489161 scopus 로고
    • Characterization of the protein import apparatus in isolated outer envelopes of chloroplasts
    • Waegemann K., and Soll J. (1991). Characterization of the protein import apparatus in isolated outer envelopes of chloroplasts Plant J. 1 149 158.
    • (1991) Plant J , vol.1 , Issue.149 , pp. 158
    • Waegemann, K.1    Soll, J.2
  • 61
    • 0004295111 scopus 로고    scopus 로고
    • Cold Spring Harbor, NY, USA: Cold Spring Harbor Laboratory Press
    • Weigel D., and Glazebrook J. (2002). Arabidopsis: A Laboratory Manual (Cold Spring Harbor, NY, USA: Cold Spring Harbor Laboratory Press), pp. 41-43.
    • (2002) Arabidopsis: A Laboratory Manual , pp. 41-43
    • Weigel, D.1    Glazebrook, J.2
  • 62
    • 65349094034 scopus 로고    scopus 로고
    • Loss of chloroplast protease SPPA function alters high light acclimation processes in Arabidopsis thaliana L. (Heynh.)
    • Wetzel, C.M., Harmacek, L.D., Yuan, L.H., Wopereis, J.L., Chubb, R., and Turini, P. (2009). Loss of chloroplast protease SPPA function alters high light acclimation processes in Arabidopsis thaliana L. (Heynh.) J. Exp. Bot, 60, 1715-727.
    • (2009) J. Exp. Bot , vol.60 , pp. 1715-1727
    • Wetzel, C.M.1    Harmacek, L.D.2    Yuan, L.H.3    Wopereis, J.L.4    Chubb, R.5    Turini, P.6
  • 63
    • 40349091686 scopus 로고    scopus 로고
    • An 'Electronic Fluorescent Pictograph' browser for exploring and analyzing large-scale biological data sets
    • Winter D. Vinegar B. Nahal H. Ammar R. Wilson G.V., and Provart N.J. (2007). An 'Electronic Fluorescent Pictograph' browser for exploring and analyzing large-scale biological data sets. PLoS One. 2, e718.
    • (2007) PLoS One , vol.2
    • Winter, D.1    Vinegar, B.2    Nahal, H.3    Ammar, R.4    Wilson, G.V.5    Provart, N.J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.