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Volumn 7, Issue FEB2016, 2016, Pages

Chloroplast iron transport proteins – Function and impact on plant physiology

Author keywords

Chloroplast; Iron transport; Membrane protein; Metal homeostasis; Transporter

Indexed keywords


EID: 84960082093     PISSN: None     EISSN: 1664462X     Source Type: Journal    
DOI: 10.3389/fpls.2016.00178     Document Type: Article
Times cited : (78)

References (100)
  • 1
    • 84958319104 scopus 로고
    • Leaf responses to Fe deficiency - A review
    • Abadia, J. (1992). Leaf responses to Fe deficiency - a review. J. Plant Nutr. 15, 1699-1713. doi: 10.1080/01904169209364432
    • (1992) J. Plant Nutr. , vol.15 , pp. 1699-1713
    • Abadia, J.1
  • 3
    • 0033513358 scopus 로고    scopus 로고
    • The water-water cycle in chloroplasts: Scavenging of active oxygen and dissipation of excess photons
    • Asada, K. (1999). The water-water cycle in chloroplasts: scavenging of active oxygen and dissipation of excess photons. Annu. Rev. Plant Physiol. Plant. Mol. Biol. 50, 601-639. doi: 10.1146/annurev.arplant.50.1.601
    • (1999) Annu. Rev. Plant Physiol. Plant. Mol. Biol. , vol.50 , pp. 601-639
    • Asada, K.1
  • 4
    • 79954416607 scopus 로고    scopus 로고
    • Ancient and essential: The assembly of iron-sulfur clusters in plants
    • Balk, J., and Pilon, M. (2011). Ancient and essential: the assembly of iron-sulfur clusters in plants. Trends Plant Sci. 16, 218-226. doi: 10.1016/j.tplants.2010.12.006
    • (2011) Trends Plant Sci. , vol.16 , pp. 218-226
    • Balk, J.1    Pilon, M.2
  • 5
    • 84899735628 scopus 로고    scopus 로고
    • Iron cofactor assembly in plants
    • Balk, J., and Schaedler, T. A. (2014). Iron cofactor assembly in plants. Annu. Rev. Plant Biol. 65, 125-153. doi: 10.1146/annurev-arplant-050213-035759
    • (2014) Annu. Rev. Plant Biol. , vol.65 , pp. 125-153
    • Balk, J.1    Schaedler, T.A.2
  • 6
    • 70349331195 scopus 로고    scopus 로고
    • Protein import machineries in endosymbiotic organelles
    • Balsera, M., Soll, J., and Bolter, B. (2009). Protein import machineries in endosymbiotic organelles. Cell. Mol. Life Sci. 66, 1903-1923. doi: 10.1007/s00018-009-8644-2
    • (2009) Cell. Mol. Life Sci. , vol.66 , pp. 1903-1923
    • Balsera, M.1    Soll, J.2    Bolter, B.3
  • 7
    • 79957574450 scopus 로고    scopus 로고
    • The rice mitochondrial iron transporter is essential for plant growth
    • Bashir, K., Ishimaru, Y., Shimo, H., Nagasaka, S., Fujimoto, M., Takanashi, H., et al. (2011). The rice mitochondrial iron transporter is essential for plant growth. Nat. Commun. 2:322. doi: 10.1038/ncomms1326
    • (2011) Nat. Commun. , vol.2 , pp. 322
    • Bashir, K.1    Ishimaru, Y.2    Shimo, H.3    Nagasaka, S.4    Fujimoto, M.5    Takanashi, H.6
  • 8
    • 0028870197 scopus 로고
    • Subcellular localization and characterization of excessive iron in the nicotianamine-less tomato mutant chloronerva
    • Becker, R., Fritz, E., and Manteuffel, R. (1995). Subcellular localization and characterization of excessive iron in the nicotianamine-less tomato mutant chloronerva. Plant Physiol. 108, 269-275.
    • (1995) Plant Physiol. , vol.108 , pp. 269-275
    • Becker, R.1    Fritz, E.2    Manteuffel, R.3
  • 9
    • 84878810097 scopus 로고    scopus 로고
    • Requirements of the cytosolic iron-sulfur cluster assembly pathway in Arabidopsis
    • Bernard, D. G., Netz, D. J., Lagny, T. J., Pierik, A. J., and Balk, J. (2013). Requirements of the cytosolic iron-sulfur cluster assembly pathway in Arabidopsis. Philos. Trans. R. Soc. Biol. Sci. 368:20120259. doi: 10.1098/rstb.2012.0259
    • (2013) Philos. Trans. R. Soc. Biol. Sci. , vol.368
    • Bernard, D.G.1    Netz, D.J.2    Lagny, T.J.3    Pierik, A.J.4    Balk, J.5
  • 10
    • 34547674885 scopus 로고    scopus 로고
    • Chloroplast envelope membranes: A dynamic interface between plastids and the cytosol
    • Block, M. A., Douce, R., Joyard, J., and Rolland, N. (2007). Chloroplast envelope membranes: a dynamic interface between plastids and the cytosol. Photosynth. Res. 92, 225-244. doi: 10.1007/s11120-007-9195-8
    • (2007) Photosynth. Res. , vol.92 , pp. 225-244
    • Block, M.A.1    Douce, R.2    Joyard, J.3    Rolland, N.4
  • 11
    • 84920179053 scopus 로고    scopus 로고
    • Iron nutrition, biomass production, and plant product quality
    • Briat, J. F., Dubos, C., and Gaymard, F. (2015). Iron nutrition, biomass production, and plant product quality. Trends Plant Sci. 20, 33-40. doi: 10.1016/j.tplants.2014.07.005
    • (2015) Trends Plant Sci. , vol.20 , pp. 33-40
    • Briat, J.F.1    Dubos, C.2    Gaymard, F.3
  • 12
    • 77953811994 scopus 로고    scopus 로고
    • Ferritins and iron storage in plants
    • Briat, J. F., Duc, C., Ravet, K., and Gaymard, F. (2010a). Ferritins and iron storage in plants. Biochim. Biophys. Acta 1800, 806-814. doi: 10.1016/j.bbagen.2009.12.003
    • (2010) Biochim. Biophys. Acta , vol.1800 , pp. 806-814
    • Briat, J.F.1    Duc, C.2    Ravet, K.3    Gaymard, F.4
  • 13
    • 77951995410 scopus 로고    scopus 로고
    • New insights into ferritin synthesis and function highlight a link between iron homeostasis and oxidative stress in plants
    • Briat, J. F., Ravet, K., Arnaud, N., Duc, C., Boucherez, J., Touraine, B., et al. (2010b). New insights into ferritin synthesis and function highlight a link between iron homeostasis and oxidative stress in plants. Ann. Bot. 105, 811-822. doi: 10.1093/aob/mcp128
    • (2010) Ann. Bot. , vol.105 , pp. 811-822
    • Briat, J.F.1    Ravet, K.2    Arnaud, N.3    Duc, C.4    Boucherez, J.5    Touraine, B.6
  • 14
    • 84922749866 scopus 로고    scopus 로고
    • Molecular mechanisms governingArabidopsis iron uptake
    • Brumbarova, T., Bauer, P., and Ivanov, R. (2015). Molecular mechanisms governingArabidopsis iron uptake. Trends Plant Sci. 20, 124-133. doi: 10.1016/j.tplants.2014.11.004
    • (2015) Trends Plant Sci. , vol.20 , pp. 124-133
    • Brumbarova, T.1    Bauer, P.2    Ivanov, R.3
  • 15
    • 0030936803 scopus 로고    scopus 로고
    • Light-dependent iron transport into isolated barley chloroplasts
    • Bughio, N., Takahashi, M., Yoshimura, E., Nishizawa, N. K., and Mori, S. (1997). Light-dependent iron transport into isolated barley chloroplasts. Plant Cell Phys. 38, 101-105. doi: 10.1093/oxfordjournals.pcp.a029079
    • (1997) Plant Cell Phys. , vol.38 , pp. 101-105
    • Bughio, N.1    Takahashi, M.2    Yoshimura, E.3    Nishizawa, N.K.4    Mori, S.5
  • 16
    • 34248634581 scopus 로고    scopus 로고
    • Molecular mechanism of ferricsiderophore passage through the outer membrane receptor proteins ofEscherichia coli
    • Chakraborty, R., Storey, E., and van der Helm, D. (2007). Molecular mechanism of ferricsiderophore passage through the outer membrane receptor proteins ofEscherichia coli. BioMetals 20, 263-274. doi: 10.1007/s10534-006-9060-9
    • (2007) BioMetals , vol.20 , pp. 263-274
    • Chakraborty, R.1    Storey, E.2    van der Helm, D.3
  • 17
    • 71249143967 scopus 로고    scopus 로고
    • Copper delivery by the copper chaperone for chloroplast and cytosolic copper/zinc-superoxide dismutases: Regulation and unexpected phenotypes in an Arabidopsis mutant
    • Cohu, C. M., Abdel-Ghany, S. E., Gogolin Reynolds, K. A., Onofrio, A. M., Bodecker, J. R., Kimbrel, J. A., et al. (2009). Copper delivery by the copper chaperone for chloroplast and cytosolic copper/zinc-superoxide dismutases: regulation and unexpected phenotypes in an Arabidopsis mutant. Mol. Plant 2, 1336-1350. doi: 10.1093/mp/ssp084
    • (2009) Mol. Plant , vol.2 , pp. 1336-1350
    • Cohu, C.M.1    Abdel-Ghany, S.E.2    Gogolin Reynolds, K.A.3    Onofrio, A.M.4    Bodecker, J.R.5    Kimbrel, J.A.6
  • 18
    • 77749328960 scopus 로고    scopus 로고
    • The MAR1 transporter is an opportunistic entry point for antibiotics
    • Conte, S., and Lloyd, A. (2010). The MAR1 transporter is an opportunistic entry point for antibiotics. Plant Signal. Behav. 5, 49-52. doi: 10.4161/psb.5.1.10142
    • (2010) Plant Signal. Behav. , vol.5 , pp. 49-52
    • Conte, S.1    Lloyd, A.2
  • 19
    • 70349651782 scopus 로고    scopus 로고
    • Multiple antibiotic resistance in Arabidopsis thaliana is conferred by mutations in a chloroplast-localized transport protein
    • Conte, S., Stevenson, D., Furner, I., and Lloyd, A. (2009). Multiple antibiotic resistance in Arabidopsis thaliana is conferred by mutations in a chloroplast-localized transport protein. Plant Physiol. 151, 559-573. doi: 10.1104/pp.109.143487
    • (2009) Plant Physiol. , vol.151 , pp. 559-573
    • Conte, S.1    Stevenson, D.2    Furner, I.3    Lloyd, A.4
  • 20
    • 84900819481 scopus 로고    scopus 로고
    • Arabidopsis thaliana yellow stripe1-Like4 and Yellow Stripe1-Like6 localize to internal cellular membranes and are involved in metal ion homeostasis
    • Conte, S. S., Chu, H. H., Rodriguez, D. C., Punshon, T., Vasques, K. A., Salt, D. E., et al. (2013). Arabidopsis thaliana yellow stripe1-Like4 and Yellow Stripe1-Like6 localize to internal cellular membranes and are involved in metal ion homeostasis. Front. Plant Sci. 4:283. doi: 10.3389/fpls.2013.00283
    • (2013) Front. Plant Sci. , vol.4 , pp. 283
    • Conte, S.S.1    Chu, H.H.2    Rodriguez, D.C.3    Punshon, T.4    Vasques, K.A.5    Salt, D.E.6
  • 21
    • 84891774934 scopus 로고    scopus 로고
    • The iron-sulfur cluster assembly machineries in plants: Current knowledge and open questions
    • Couturier, J., Touraine, B., Briat, J. F., Gaymard, F., and Rouhier, N. (2013). The iron-sulfur cluster assembly machineries in plants: current knowledge and open questions.Front. Plant Sci. 4:259. doi: 10.3389/fpls.2013.00259
    • (2013) Front. Plant Sci. , vol.4 , pp. 259
    • Couturier, J.1    Touraine, B.2    Briat, J.F.3    Gaymard, F.4    Rouhier, N.5
  • 22
    • 57749169737 scopus 로고    scopus 로고
    • Metal movement within the plant: Contribution of nicotianamine and yellow stripe 1-like transporters
    • Curie, C., Cassin, G., Couch, D., Divol, F., Higuchi, K., Le Jean, M., et al. (2009). Metal movement within the plant: contribution of nicotianamine and yellow stripe 1-like transporters. Annals Bot. 103, 1-11. doi: 10.1093/aob/mcn207
    • (2009) Annals Bot. , vol.103 , pp. 1-11
    • Curie, C.1    Cassin, G.2    Couch, D.3    Divol, F.4    Higuchi, K.5    Le Jean, M.6
  • 23
    • 84876777659 scopus 로고    scopus 로고
    • TheArabidopsis YELLOW STRIPE LIKE4 and 6 transporters control iron release from the chloroplast
    • Divol, F., Couch, D., Conéjéro, G., Roschzttardtz, H., Mari, S., and Curie, C. (2013). TheArabidopsis YELLOW STRIPE LIKE4 and 6 transporters control iron release from the chloroplast. Plant Cell 25, 1040-1055. doi: 10.1105/tpc.112.107672
    • (2013) Plant Cell , vol.25 , pp. 1040-1055
    • Divol, F.1    Couch, D.2    Conéjéro, G.3    Roschzttardtz, H.4    Mari, S.5    Curie, C.6
  • 24
    • 34547876870 scopus 로고    scopus 로고
    • Solute channels of the outer membrane: From bacteria to chloroplasts
    • Duy, D., Soll, J., and Philippar, K. (2007a). Solute channels of the outer membrane: from bacteria to chloroplasts. Biol. Chem. 388, 879-889. doi: 10.1515/BC.2007.120
    • (2007) Biol. Chem. , vol.388 , pp. 879-889
    • Duy, D.1    Soll, J.2    Philippar, K.3
  • 25
    • 34248146824 scopus 로고    scopus 로고
    • PIC1, an ancient permease in Arabidopsis chloroplasts, mediates iron transport
    • Duy, D., Wanner, G., Meda, A. R., von Wirén, N., Soll, J., and Philippar, K. (2007b). PIC1, an ancient permease in Arabidopsis chloroplasts, mediates iron transport. Plant Cell 19, 986-1006. doi: 10.1105/tpc.106.047407
    • (2007) Plant Cell , vol.19 , pp. 986-1006
    • Duy, D.1    Wanner, G.2    Meda, A.R.3    von Wirén, N.4    Soll, J.5    Philippar, K.6
  • 26
    • 79953692401 scopus 로고    scopus 로고
    • The chloroplast permease PIC1 regulates plant growth and development by directing homeostasis and transport of iron
    • Duy, D., Stübe, R., Wanner, G., and Philippar, K. (2011). The chloroplast permease PIC1 regulates plant growth and development by directing homeostasis and transport of iron. Plant Physiol. 155, 1709-1722. doi: 10.1104/pp.110.170233
    • (2011) Plant Physiol. , vol.155 , pp. 1709-1722
    • Duy, D.1    Stübe, R.2    Wanner, G.3    Philippar, K.4
  • 27
    • 24744437494 scopus 로고    scopus 로고
    • Secondary transporters for nickel and cobalt ions: Theme and variations
    • Eitinger, T., Suhr, J., Moore, L., and Smith, J. A. (2005). Secondary transporters for nickel and cobalt ions: theme and variations. BioMetals 18, 399-405. doi: 10.1007/s10534-005-3714-x
    • (2005) BioMetals , vol.18 , pp. 399-405
    • Eitinger, T.1    Suhr, J.2    Moore, L.3    Smith, J.A.4
  • 28
    • 77953149231 scopus 로고    scopus 로고
    • AT_CHLORO, a comprehensive chloroplast proteome database with subplastidial localization and curated information on envelope proteins
    • Ferro, M., Brugière, S., Salvi, D., Seigneurin-Berny, D., Court, M., Moyet, L., et al. (2010). AT_CHLORO, a comprehensive chloroplast proteome database with subplastidial localization and curated information on envelope proteins. Mol. Cell. Proteomics 9, 1063-1084. doi: 10.1074/mcp.M900325-MCP200
    • (2010) Mol. Cell. Proteomics , vol.9 , pp. 1063-1084
    • Ferro, M.1    Brugière, S.2    Salvi, D.3    Seigneurin-Berny, D.4    Court, M.5    Moyet, L.6
  • 30
    • 79953727247 scopus 로고    scopus 로고
    • The import and export business in plastids: Transport processes across the inner envelope membrane
    • Fischer, K. (2011). The import and export business in plastids: transport processes across the inner envelope membrane. Plant Physiol. 155, 1511-1519. doi: 10.1104/pp.110.170241
    • (2011) Plant Physiol. , vol.155 , pp. 1511-1519
    • Fischer, K.1
  • 31
    • 84940277105 scopus 로고    scopus 로고
    • Tobacco PIC1 mediates iron transport and regulates chloroplast development
    • Gong, X., Guo, C., Terachi, T., Cai, H., and Yu, D. (2015). Tobacco PIC1 mediates iron transport and regulates chloroplast development. Plant Mol. Biol. Rep. 33, 401-413. doi: 10.1007/s11105-014-0758-5
    • (2015) Plant Mol. Biol. Rep. , vol.33 , pp. 401-413
    • Gong, X.1    Guo, C.2    Terachi, T.3    Cai, H.4    Yu, D.5
  • 33
    • 58149513082 scopus 로고    scopus 로고
    • Revaluating the evolution of the Toc and Tic protein translocons
    • Gross, J., and Bhattacharya, D. (2009). Revaluating the evolution of the Toc and Tic protein translocons. Trends Plant Sci. 14, 13-20. doi: 10.1016/j.tplants.2008.10.003
    • (2009) Trends Plant Sci. , vol.14 , pp. 13-20
    • Gross, J.1    Bhattacharya, D.2
  • 34
    • 84902089812 scopus 로고    scopus 로고
    • The distinct functional roles of the inner and outer chloroplast envelope of Pea (Pisum sativum) as revealed by proteomic approaches
    • Gutierrez-Carbonell, E., Takahashi, D., Lattanzio, G., Rodríguez-Celma, J., Kehr, J., Soll, J., et al. (2014). The distinct functional roles of the inner and outer chloroplast envelope of Pea (Pisum sativum) as revealed by proteomic approaches. J. Proteome Res. 13, 2941-2953. doi: 10.1021/pr500106s
    • (2014) J. Proteome Res. , vol.13 , pp. 2941-2953
    • Gutierrez-Carbonell, E.1    Takahashi, D.2    Lattanzio, G.3    Rodríguez-Celma, J.4    Kehr, J.5    Soll, J.6
  • 35
    • 0026740508 scopus 로고
    • Biologically relevant metal ion-dependent hydroxyl radical generation - An update
    • Halliwell, B., and Gutteridge, J. M. C. (1992). Biologically relevant metal ion-dependent hydroxyl radical generation - an update. FEBS Lett. 307, 108-112. doi: 10.1016/0014-5793(92)80911-Y
    • (1992) FEBS Lett. , vol.307 , pp. 108-112
    • Halliwell, B.1    Gutteridge, J.M.C.2
  • 36
    • 70350400609 scopus 로고    scopus 로고
    • Maize ZmFDR3 localized in chloroplasts is involved in iron transport
    • Han, J., Song, X., Li, P., Yang, H., and Yin, L. (2009). Maize ZmFDR3 localized in chloroplasts is involved in iron transport. Sci. China C Life Sci. 52, 864-871. doi: 10.1007/s11427-009-0108-2
    • (2009) Sci. China C Life Sci. , vol.52 , pp. 864-871
    • Han, J.1    Song, X.2    Li, P.3    Yang, H.4    Yin, L.5
  • 37
    • 84859047219 scopus 로고    scopus 로고
    • Vacuolar nicotianamine has critical and distinct roles under iron deficiency and for zinc sequestration in Arabidopsis
    • Haydon, M. J., Kawachi, M., Wirtz, M., Hillmer, S., Hell, R., and Krämer, U. (2012). Vacuolar nicotianamine has critical and distinct roles under iron deficiency and for zinc sequestration in Arabidopsis. Plant Cell 24, 724-737. doi: 10.1105/tpc.111.095042
    • (2012) Plant Cell , vol.24 , pp. 724-737
    • Haydon, M.J.1    Kawachi, M.2    Wirtz, M.3    Hillmer, S.4    Hell, R.5    Krämer, U.6
  • 38
    • 46249121083 scopus 로고    scopus 로고
    • Protein trafficking to plastids: One theme, many variations
    • Inaba, T., and Schnell, D. J. (2008). Protein trafficking to plastids: one theme, many variations. Biochem. J. 413, 15-28. doi: 10.1042/BJ20080490
    • (2008) Biochem. J. , vol.413 , pp. 15-28
    • Inaba, T.1    Schnell, D.J.2
  • 39
    • 48749114297 scopus 로고    scopus 로고
    • Chloroplast Fe(III) chelate reductase activity is essential for seedling viability under iron limiting conditions
    • Jeong, J., Cohu, C., Kerkeb, L., Pilon, M., Connolly, E. L., and Guerinot, M. L. (2008). Chloroplast Fe(III) chelate reductase activity is essential for seedling viability under iron limiting conditions. Proc. Natl. Acad. Sci. U.S.A. 105, 10619-10624. doi: 10.1073/pnas.0708367105
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 10619-10624
    • Jeong, J.1    Cohu, C.2    Kerkeb, L.3    Pilon, M.4    Connolly, E.L.5    Guerinot, M.L.6
  • 40
    • 84873880804 scopus 로고    scopus 로고
    • Uncovering the protein translocon at the chloroplast inner envelope membrane
    • Kikuchi, S., Bédard, J., Hirano, M., Hirabayashi, Y., Oishi, M., Imai, M., et al. (2013). Uncovering the protein translocon at the chloroplast inner envelope membrane.Science 339, 571-574. doi: 10.1126/science.1229262
    • (2013) Science , vol.339 , pp. 571-574
    • Kikuchi, S.1    Bédard, J.2    Hirano, M.3    Hirabayashi, Y.4    Oishi, M.5    Imai, M.6
  • 41
    • 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. doi: 10.1105/tpc.108.063552
    • (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
  • 42
    • 33751573050 scopus 로고    scopus 로고
    • Localization of iron in Arabidopsis seed requires the vacuolar membrane transporter VIT1
    • Kim, S. A., Punshon, T., Lanzirotti, A., Li, L., Alonso, J. M., Ecker, J. R., et al. (2006). Localization of iron in Arabidopsis seed requires the vacuolar membrane transporter VIT1. Science 314, 1295-1298. doi: 10.1126/science.1132563
    • (2006) Science , vol.314 , pp. 1295-1298
    • Kim, S.A.1    Punshon, T.2    Lanzirotti, A.3    Li, L.4    Alonso, J.M.5    Ecker, J.R.6
  • 43
    • 84864320486 scopus 로고    scopus 로고
    • Iron uptake, translocation, and regulation in higher plants
    • Kobayashi, T., and Nishizawa, N. K. (2012). Iron uptake, translocation, and regulation in higher plants. Annu. Rev. Plant Biol. 63, 131-152. doi: 10.1146/annurev-arplant-042811-105522
    • (2012) Annu. Rev. Plant Biol. , vol.63 , pp. 131-152
    • Kobayashi, T.1    Nishizawa, N.K.2
  • 44
    • 84893005887 scopus 로고    scopus 로고
    • Coordinated transporter activity shapes high-affinity iron acquisition in cyanobacteria
    • Kranzler, C., Lis, H., Finkel, O. M., Schmetterer, G., Shaked, Y., and Keren, N. (2014). Coordinated transporter activity shapes high-affinity iron acquisition in cyanobacteria.ISME J. 8, 409-417. doi: 10.1038/ismej.2013.161
    • (2014) ISME J. , vol.8 , pp. 409-417
    • Kranzler, C.1    Lis, H.2    Finkel, O.M.3    Schmetterer, G.4    Shaked, Y.5    Keren, N.6
  • 46
    • 77952161465 scopus 로고    scopus 로고
    • ZEBRA-NECROSIS, a thylakoid-bound protein, is critical for the photoprotection of developing chloroplasts during early leaf development
    • Li, J., Pandeya, D., Nath, K., Zulfugarov, I. S., Yoo, S. C., Zhang, H., et al. (2010). ZEBRA-NECROSIS, a thylakoid-bound protein, is critical for the photoprotection of developing chloroplasts during early leaf development. Plant J. 62, 713-725. doi: 10.1111/j.1365-313X.2010.04183.x
    • (2010) Plant J. , vol.62 , pp. 713-725
    • Li, J.1    Pandeya, D.2    Nath, K.3    Zulfugarov, I.S.4    Yoo, S.C.5    Zhang, H.6
  • 48
    • 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., and Yang, Z. N. (2009). Translocons on the inner and outer envelopes of chloroplasts share similar evolutionary origin in Arabidopsis thaliana. J. Evol. Biol. 22, 1418-1428. doi: 10.1111/j.1420-9101.2009.01755.x
    • (2009) J. Evol. Biol. , vol.22 , pp. 1418-1428
    • Lv, H.X.1    Guo, G.Q.2    Yang, Z.N.3
  • 49
    • 84940922533 scopus 로고    scopus 로고
    • Bypassing iron storage in endodermal vacuoles rescues the iron mobilization defect in the natural resistance associated-macrophage protein3/natural resistance associated-macrophage protein4 double mutant
    • Mary, V., Schnell Ramos, M., Gillet, C., Socha, A. L., Giraudat, J., Agorio, A., et al. (2015). Bypassing iron storage in endodermal vacuoles rescues the iron mobilization defect in the natural resistance associated-macrophage protein3/natural resistance associated-macrophage protein4 double mutant. Plant Physiol. 169, 748-759. doi: 10.1104/pp.15.00380
    • (2015) Plant Physiol. , vol.169 , pp. 748-759
    • Mary, V.1    Schnell Ramos, M.2    Gillet, C.3    Socha, A.L.4    Giraudat, J.5    Agorio, A.6
  • 50
    • 79955130989 scopus 로고    scopus 로고
    • Allocation of Fe and ferric chelate reductase activities in mesophyll cells of barley and sorghum under Fe-deficient conditions
    • Mikami, Y., Saito, A., Miwa, E., and Higuchi, K. (2011). Allocation of Fe and ferric chelate reductase activities in mesophyll cells of barley and sorghum under Fe-deficient conditions. Plant Physiol. Biochem. 49, 513-519. doi: 10.1016/j.plaphy.2011.01.009
    • (2011) Plant Physiol. Biochem. , vol.49 , pp. 513-519
    • Mikami, Y.1    Saito, A.2    Miwa, E.3    Higuchi, K.4
  • 51
    • 0035900736 scopus 로고    scopus 로고
    • The Rieske Fe/S protein of the cytochrome b6/f complex in chloroplasts: Missing link in the evolution of protein transport pathways in chloroplasts?
    • Molik, S., Karnauchov, I., Weidlich, C., Herrmann, R. G., and Klosgen, R. B. (2001). The Rieske Fe/S protein of the cytochrome b6/f complex in chloroplasts: missing link in the evolution of protein transport pathways in chloroplasts? J. Biol. Chem. 276, 42761-42766. doi: 10.1074/jbc.M106690200
    • (2001) J. Biol. Chem. , vol.276 , pp. 42761-42766
    • Molik, S.1    Karnauchov, I.2    Weidlich, C.3    Herrmann, R.G.4    Klosgen, R.B.5
  • 52
    • 72049114946 scopus 로고    scopus 로고
    • The ferroportin metal efflux proteins function in iron and cobalt homeostasis inArabidopsis
    • Morrissey, J., Baxter, I. R., Lee, J., Li, L., Lahner, B., Grotz, N., et al. (2009). The ferroportin metal efflux proteins function in iron and cobalt homeostasis inArabidopsis. Plant Cell 21, 3326-3338. doi: 10.1105/tpc.109.069401
    • (2009) Plant Cell , vol.21 , pp. 3326-3338
    • Morrissey, J.1    Baxter, I.R.2    Lee, J.3    Li, L.4    Lahner, B.5    Grotz, N.6
  • 53
    • 70350212547 scopus 로고    scopus 로고
    • Iron uptake and transport in plants: The good, the bad, and the ionome
    • Morrissey, J., and Guerinot, M. L. (2009). Iron uptake and transport in plants: the good, the bad, and the ionome. Chem. Rev. 109, 4553-4567. doi: 10.1021/cr900112r
    • (2009) Chem. Rev. , vol.109 , pp. 4553-4567
    • Morrissey, J.1    Guerinot, M.L.2
  • 54
    • 12244262259 scopus 로고    scopus 로고
    • Adaptation to Fe-deficiency requires remodeling of the photosynthetic apparatus
    • Moseley, J. L., Allinger, T., Herzog, S., Hoerth, P., Wehinger, E., Merchant, S., et al. (2002). Adaptation to Fe-deficiency requires remodeling of the photosynthetic apparatus. EMBO J. 21, 6709-6720. doi: 10.1093/emboj/cdf666
    • (2002) EMBO J. , vol.21 , pp. 6709-6720
    • Moseley, J.L.1    Allinger, T.2    Herzog, S.3    Hoerth, P.4    Wehinger, E.5    Merchant, S.6
  • 56
    • 33646410449 scopus 로고    scopus 로고
    • Expression profiling of the Arabidopsis ferric chelate reductase (FRO) gene family reveals differential regulation by iron and copper
    • Mukherjee, I., Campbell, N., Ash, J., and Connolly, E. (2006). Expression profiling of the Arabidopsis ferric chelate reductase (FRO) gene family reveals differential regulation by iron and copper. Planta 223, 1178-1190. doi: 10.1007/s00425-005-0165-0
    • (2006) Planta , vol.223 , pp. 1178-1190
    • Mukherjee, I.1    Campbell, N.2    Ash, J.3    Connolly, E.4
  • 57
    • 84930614158 scopus 로고    scopus 로고
    • Analysis of Arabidopsis thaliana atfer4-1, atfh and atfer4-1/atfh mutants uncovers frataxin and ferritin contributions to leaf ionome homeostasis
    • Murgia, I., and Vigani, G. (2015). Analysis of Arabidopsis thaliana atfer4-1, atfh and atfer4-1/atfh mutants uncovers frataxin and ferritin contributions to leaf ionome homeostasis. Plant Physiol. Biochem. 94, 65-72. doi: 10.1016/j.plaphy.2015.05.011
    • (2015) Plant Physiol. Biochem. , vol.94 , pp. 65-72
    • Murgia, I.1    Vigani, G.2
  • 58
    • 84935003389 scopus 로고    scopus 로고
    • The TIC complex uncovered: The alternative view on the molecular mechanism of protein translocation across the inner envelope membrane of chloroplasts
    • Nakai, M. (2015). The TIC complex uncovered: the alternative view on the molecular mechanism of protein translocation across the inner envelope membrane of chloroplasts. Biochim. Biophys. Acta 1847, 957-967. doi: 10.1016/j.bbabio.2015.02.011
    • (2015) Biochim. Biophys. Acta , vol.1847 , pp. 957-967
    • Nakai, M.1
  • 59
    • 36048942406 scopus 로고    scopus 로고
    • Comparative quantitative proteomics to investigate the remodeling of bioenergetic pathways under iron deficiency in Chlamydomonas reinhardtii
    • Naumann, B., Busch, A., Allmer, J., Ostendorf, E., Zeller, M., Kirchhoff, H., et al. (2007). Comparative quantitative proteomics to investigate the remodeling of bioenergetic pathways under iron deficiency in Chlamydomonas reinhardtii. Proteomics 7, 3964-3979. doi: 10.1002/pmic.200700407
    • (2007) Proteomics , vol.7 , pp. 3964-3979
    • Naumann, B.1    Busch, A.2    Allmer, J.3    Ostendorf, E.4    Zeller, M.5    Kirchhoff, H.6
  • 60
    • 84863325942 scopus 로고    scopus 로고
    • Characterization of Arabidopsis NEET reveals an ancient role for NEET proteins in iron metabolism
    • Nechushtai, R., Conlan, A. R., Harir, Y., Song, L., Yogev, O., Eisenberg-Domovich, Y., et al. (2012). Characterization of Arabidopsis NEET reveals an ancient role for NEET proteins in iron metabolism. Plant Cell 24, 2139-2154. doi: 10.1105/tpc.112.097634
    • (2012) Plant Cell , vol.24 , pp. 2139-2154
    • Nechushtai, R.1    Conlan, A.R.2    Harir, Y.3    Song, L.4    Yogev, O.5    Eisenberg-Domovich, Y.6
  • 61
    • 79959901177 scopus 로고    scopus 로고
    • Chloroplastic and mitochondrial metal homeostasis
    • Nouet, C., Motte, P., and Hanikenne, M. (2011). Chloroplastic and mitochondrial metal homeostasis. Trends Plant Sci. 16, 395-404. doi: 10.1016/j.tplants.2011.03.005
    • (2011) Trends Plant Sci. , vol.16 , pp. 395-404
    • Nouet, C.1    Motte, P.2    Hanikenne, M.3
  • 62
    • 0035504261 scopus 로고    scopus 로고
    • Structure and differential expression of the four members of the Arabidopsis thaliana ferritin gene family
    • Petit, J. M., Briat, J. F., and Lobreaux, S. (2001). Structure and differential expression of the four members of the Arabidopsis thaliana ferritin gene family. Biochem. J. 359, 575-582. doi: 10.1042/bj3590575
    • (2001) Biochem. J. , vol.359 , pp. 575-582
    • Petit, J.M.1    Briat, J.F.2    Lobreaux, S.3
  • 64
    • 84901041391 scopus 로고    scopus 로고
    • Autophagy as a possible mechanism for micronutrient remobilization from leaves to seeds
    • Pottier, M., Masclaux-Daubresse, C., Yoshimoto, K., and Thomine, S. (2014). Autophagy as a possible mechanism for micronutrient remobilization from leaves to seeds. Front. Plant Sci. 5:11. doi: 10.3389/fpls.2014.00011
    • (2014) Front. Plant Sci. , vol.5 , pp. 11
    • Pottier, M.1    Masclaux-Daubresse, C.2    Yoshimoto, K.3    Thomine, S.4
  • 66
    • 58849163578 scopus 로고    scopus 로고
    • Ferritins control interaction between iron homeostasis and oxidative stress inArabidopsis
    • Ravet, K., Touraine, B., Boucherez, J., Briat, J. F., Gaymard, F., and Cellier, F. (2009a). Ferritins control interaction between iron homeostasis and oxidative stress inArabidopsis. Plant J. 57, 400-412. doi: 10.1111/j.1365-313X.2008.03698.x
    • (2009) Plant J. , vol.57 , pp. 400-412
    • Ravet, K.1    Touraine, B.2    Boucherez, J.3    Briat, J.F.4    Gaymard, F.5    Cellier, F.6
  • 67
    • 70349598131 scopus 로고    scopus 로고
    • Post-translational regulation of AtFER2 ferritin in response to intracellular iron trafficking during fruit development in Arabidopsis
    • Ravet, K., Touraine, B., Kim, S. A., Cellier, F., Thomine, S., Guerinot, M. L., et al. (2009b). Post-translational regulation of AtFER2 ferritin in response to intracellular iron trafficking during fruit development in Arabidopsis. Mol. Plant 2, 1095-1106. doi: 10.1093/mp/ssp041
    • (2009) Mol. Plant , vol.2 , pp. 1095-1106
    • Ravet, K.1    Touraine, B.2    Kim, S.A.3    Cellier, F.4    Thomine, S.5    Guerinot, M.L.6
  • 69
    • 33748756207 scopus 로고    scopus 로고
    • AtIREG2 encodes a tonoplast transport protein involved in iron-dependent nickel detoxification in Arabidopsis thaliana roots
    • Schaaf, G., Honsbein, A., Meda, A. R., Kirchner, S., Wipf, D., and von Wirén, N. (2006). AtIREG2 encodes a tonoplast transport protein involved in iron-dependent nickel detoxification in Arabidopsis thaliana roots. J. Biol. Chem. 281, 25532-25540. doi: 10.1074/jbc.M601062200
    • (2006) J. Biol. Chem. , vol.281 , pp. 25532-25540
    • Schaaf, G.1    Honsbein, A.2    Meda, A.R.3    Kirchner, S.4    Wipf, D.5    von Wirén, N.6
  • 70
    • 84906545328 scopus 로고    scopus 로고
    • A conserved mitochondrial ATP-binding cassette transporter exports glutathione polysulfide for cytosolic metal cofactor assembly
    • Schaedler, T. A., Thornton, J. D., Kruse, I., Schwarzländer, M., Meyer, A. J., van Veen, H. W., et al. (2014). A conserved mitochondrial ATP-binding cassette transporter exports glutathione polysulfide for cytosolic metal cofactor assembly. J. Biol. Chem.289, 23264-23274. doi: 10.1074/jbc.M114.553438
    • (2014) J. Biol. Chem. , vol.289 , pp. 23264-23274
    • Schaedler, T.A.1    Thornton, J.D.2    Kruse, I.3    Schwarzländer, M.4    Meyer, A.J.5    van Veen, H.W.6
  • 72
    • 45849123222 scopus 로고    scopus 로고
    • A cytosolic iron chaperone that delivers iron to ferritin
    • Shi, H., Bencze, K. Z., Stemmler, T. L., and Philpott, C. C. (2008). A cytosolic iron chaperone that delivers iron to ferritin. Science 320, 1207-1210. doi: 10.1126/science.1157643
    • (2008) Science , vol.320 , pp. 1207-1210
    • Shi, H.1    Bencze, K.Z.2    Stemmler, T.L.3    Philpott, C.C.4
  • 73
    • 77954055112 scopus 로고    scopus 로고
    • Disruption of Nap14, a plastid-localized non-intrinsic ABC protein in Arabidopsis thaliana results in the over-accumulation of transition metals and in aberrant chloroplast structures
    • Shimoni-Shor, E., Hassidim, M., Yuval-Naeh, N., and Keren, N. (2010). Disruption of Nap14, a plastid-localized non-intrinsic ABC protein in Arabidopsis thaliana results in the over-accumulation of transition metals and in aberrant chloroplast structures.Plant Cell Environ. 33, 1029-1038. doi: 10.1111/j.1365-3040.2010.02124.x
    • (2010) Plant Cell Environ. , vol.33 , pp. 1029-1038
    • Shimoni-Shor, E.1    Hassidim, M.2    Yuval-Naeh, N.3    Keren, N.4
  • 74
    • 0035450560 scopus 로고    scopus 로고
    • Direct measurement of ferrous ion transport across membranes using a sensitive fluorometric assay
    • Shingles, R., North, M., and McCarty, R. E. (2001). Direct measurement of ferrous ion transport across membranes using a sensitive fluorometric assay. Anal. Biochem. 296, 106-113. doi: 10.1006/abio.2001.5209
    • (2001) Anal. Biochem. , vol.296 , pp. 106-113
    • Shingles, R.1    North, M.2    McCarty, R.E.3
  • 75
    • 0036006057 scopus 로고    scopus 로고
    • Ferrous ion transport across chloroplast inner envelope membranes
    • Shingles, R., North, M., and McCarty, R. E. (2002). Ferrous ion transport across chloroplast inner envelope membranes. Plant Physiol. 128, 1022-1030. doi: 10.1104/pp.010858
    • (2002) Plant Physiol. , vol.128 , pp. 1022-1030
    • Shingles, R.1    North, M.2    McCarty, R.E.3
  • 77
    • 84898032353 scopus 로고    scopus 로고
    • Functional characterization of the chloroplast ferric chelate oxidoreductase enzyme
    • Solti, A., Muller, B., Czech, V., Sarvari, E., and Fodor, F. (2014). Functional characterization of the chloroplast ferric chelate oxidoreductase enzyme. New Phytol.202, 920-928. doi: 10.1111/nph.12715
    • (2014) New Phytol. , vol.202 , pp. 920-928
    • Solti, A.1    Muller, B.2    Czech, V.3    Sarvari, E.4    Fodor, F.5
  • 78
    • 0001618202 scopus 로고
    • Limiting factors in photosynthesis: II. Iron stress diminishes photochemical capacity by reducing the number of photosynthetic units
    • Spiller, S., and Terry, N. (1980). Limiting factors in photosynthesis: II. Iron stress diminishes photochemical capacity by reducing the number of photosynthetic units.Plant Physiol. 65, 121-125. doi: 10.1104/pp.65.1.121
    • (1980) Plant Physiol. , vol.65 , pp. 121-125
    • Spiller, S.1    Terry, N.2
  • 79
    • 84884366360 scopus 로고    scopus 로고
    • Purification and biochemical characterization of Arabidopsis At-NEET, an ancient iron-sulfur protein, reveals a conserved cleavage motif for subcellular localization
    • Su, L. W., Chang, S. H., Li, M. Y., Huang, H. Y., Jane, W. N., and Yang, J. Y. (2013). Purification and biochemical characterization of Arabidopsis At-NEET, an ancient iron-sulfur protein, reveals a conserved cleavage motif for subcellular localization. Plant Sci.213, 46-54. doi: 10.1016/j.plantsci.2013.09.001
    • (2013) Plant Sci. , vol.213 , pp. 46-54
    • Su, L.W.1    Chang, S.H.2    Li, M.Y.3    Huang, H.Y.4    Jane, W.N.5    Yang, J.Y.6
  • 80
    • 0034813188 scopus 로고    scopus 로고
    • Leaf-specific upregulation of chloroplast translocon genes by a CCT motif-containing protein. CIA 2
    • Sun, C. W., Chen, L. J., Lin, L. C., and Li, H. M. (2001). Leaf-specific upregulation of chloroplast translocon genes by a CCT motif-containing protein. CIA 2. Plant Cell 13, 2053-2061. doi: 10.1105/tpc.13.9.2053
    • (2001) Plant Cell , vol.13 , pp. 2053-2061
    • Sun, C.W.1    Chen, L.J.2    Lin, L.C.3    Li, H.M.4
  • 81
    • 77649190434 scopus 로고    scopus 로고
    • Knocking out of the mitochondrial AtFer4 ferritin does not alter response of Arabidopsis plants to abiotic stresses
    • Tarantino, D., Casagrande, F., Soave, C., and Murgia, I. (2010). Knocking out of the mitochondrial AtFer4 ferritin does not alter response of Arabidopsis plants to abiotic stresses. J. Plant Physiol. 167, 453-460. doi: 10.1016/j.jplph.2009.10.015
    • (2010) J. Plant Physiol. , vol.167 , pp. 453-460
    • Tarantino, D.1    Casagrande, F.2    Soave, C.3    Murgia, I.4
  • 82
    • 79955130979 scopus 로고    scopus 로고
    • Identification of an Arabidopsis mitoferrinlike carrier protein involved in Fe metabolism
    • Tarantino, D., Morandini, P., Ramirez, L., Soave, C., and Murgia, I. (2011). Identification of an Arabidopsis mitoferrinlike carrier protein involved in Fe metabolism. Plant Physiol. Biochem. 49, 520-529. doi: 10.1016/j.plaphy.2011.02.003
    • (2011) Plant Physiol. Biochem. , vol.49 , pp. 520-529
    • Tarantino, D.1    Morandini, P.2    Ramirez, L.3    Soave, C.4    Murgia, I.5
  • 83
    • 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. doi: 10.1105/tpc.106.044305
    • (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
  • 84
    • 0005078847 scopus 로고
    • Leaf chlorophyll content and its relation to the intracellular location of iron
    • Terry, N., and Low, G. (1982). Leaf chlorophyll content and its relation to the intracellular location of iron. J. Plant Nutr. 5, 301-310. doi: 10.1080/01904168209362959
    • (1982) J. Plant Nutr. , vol.5 , pp. 301-310
    • Terry, N.1    Low, G.2
  • 85
    • 0038468540 scopus 로고    scopus 로고
    • AtNRAMP3, a multispecific vacuolar metal transporter involved in plant responses to iron deficiency
    • Thomine, S., Lelievre, F., Debarbieux, E., Schroeder, J. I., and Barbier-Brygoo, H. (2003). AtNRAMP3, a multispecific vacuolar metal transporter involved in plant responses to iron deficiency. Plant J. 34, 685-695. doi: 10.1046/j.1365-313X.2003.01760.x
    • (2003) Plant J. , vol.34 , pp. 685-695
    • Thomine, S.1    Lelievre, F.2    Debarbieux, E.3    Schroeder, J.I.4    Barbier-Brygoo, H.5
  • 86
    • 84878966012 scopus 로고    scopus 로고
    • Iron transport in plants: Better be safe than sorry
    • Thomine, S., and Vert, G. (2013). Iron transport in plants: better be safe than sorry.Curr. Opin. Plant Biol. 16, 322-327. doi: 10.1016/j.pbi.2013.01.003
    • (2013) Curr. Opin. Plant Biol. , vol.16 , pp. 322-327
    • Thomine, S.1    Vert, G.2
  • 87
    • 40849124801 scopus 로고    scopus 로고
    • Host origin of plastid solute transporters in the first photosynthetic eukaryotes
    • Tyra, H. M., Linka, M., Weber, A. P. M., and Bhattacharya, D. (2007). Host origin of plastid solute transporters in the first photosynthetic eukaryotes. Genome Biol. 8:R212. doi: 10.1186/gb-2007-8-10-r212
    • (2007) Genome Biol. , vol.8
    • Tyra, H.M.1    Linka, M.2    Weber, A.P.M.3    Bhattacharya, D.4
  • 89
    • 41649116602 scopus 로고    scopus 로고
    • Plant ABC proteins - A unified nomenclature and updated inventory
    • Verrier, P. J., Bird, D., Burla, B., Dassa, E., Forestier, C., Geisler, M., et al. (2008). Plant ABC proteins - a unified nomenclature and updated inventory. Trends Plant Sci. 13, 151-159. doi: 10.1016/j.tplants.2008.02.001
    • (2008) Trends Plant Sci. , vol.13 , pp. 151-159
    • Verrier, P.J.1    Bird, D.2    Burla, B.3    Dassa, E.4    Forestier, C.5    Geisler, M.6
  • 90
    • 61649091369 scopus 로고    scopus 로고
    • Iron availability affects the function of mitochondria in cucumber roots
    • Vigani, G., Maffi, D., and Zocchi, G. (2009). Iron availability affects the function of mitochondria in cucumber roots. New Phytol. 182, 127-136. doi: 10.1111/j.1469-8137.2008.02747.x
    • (2009) New Phytol. , vol.182 , pp. 127-136
    • Vigani, G.1    Maffi, D.2    Zocchi, G.3
  • 91
    • 77950189767 scopus 로고    scopus 로고
    • Effect of Fe deficiency on mitochondrial alternative NAD(P)H dehydrogenases in cucumber roots
    • Vigani, G., and Zocchi, G. (2010). Effect of Fe deficiency on mitochondrial alternative NAD(P)H dehydrogenases in cucumber roots. J. Plant Physiol. 167, 666-669. doi: 10.1016/j.jplph.2009.12.006
    • (2010) J. Plant Physiol. , vol.167 , pp. 666-669
    • Vigani, G.1    Zocchi, G.2
  • 92
    • 84878529093 scopus 로고    scopus 로고
    • Signals from chloroplasts and mitochondria for iron homeostasis regulation
    • Vigani, G., Zocchi, G., Bashir, K., Philippar, K., and Briat, J. F. (2013). Signals from chloroplasts and mitochondria for iron homeostasis regulation. Trends Plant Sci. 18, 305-311. doi: 10.1016/j.tplants.2013.01.006
    • (2013) Trends Plant Sci. , vol.18 , pp. 305-311
    • Vigani, G.1    Zocchi, G.2    Bashir, K.3    Philippar, K.4    Briat, J.F.5
  • 93
    • 67650149292 scopus 로고    scopus 로고
    • Chloroplasts autophagy during senescence of individually darkened leaves
    • Wada, S., and Ishida, H. (2009). Chloroplasts autophagy during senescence of individually darkened leaves. Plant Signal. Behav. 4, 565-567. doi: 10.4161/psb.4.6.8877
    • (2009) Plant Signal. Behav. , vol.4 , pp. 565-567
    • Wada, S.1    Ishida, H.2
  • 94
    • 49249121105 scopus 로고    scopus 로고
    • Quantitative trait locus mapping for seed mineral concentrations in two Arabidopsis thaliana recombinant inbred populations
    • Waters, B. M., and Grusak, M. A. (2008). Quantitative trait locus mapping for seed mineral concentrations in two Arabidopsis thaliana recombinant inbred populations.New Phytol. 179, 1033-1047. doi: 10.1111/j.1469-8137.2008.02544.x
    • (2008) New Phytol. , vol.179 , pp. 1033-1047
    • Waters, B.M.1    Grusak, M.A.2
  • 95
    • 79955583888 scopus 로고    scopus 로고
    • Connecting the plastid: Transporters of the plastid envelope and their role in linking plastidial with cytosolic metabolism
    • Weber, A. P., and Linka, N. (2011). Connecting the plastid: transporters of the plastid envelope and their role in linking plastidial with cytosolic metabolism. Annu. Rev. Plant Biol. 62, 53-77. doi: 10.1146/annurev-arplant-042110-103903
    • (2011) Annu. Rev. Plant Biol. , vol.62 , pp. 53-77
    • Weber, A.P.1    Linka, N.2
  • 96
    • 2942659075 scopus 로고    scopus 로고
    • AtNAP7 is a plastidic SufC-like ATP-binding cassette/ATPase essential for Arabidopsis embryogenesis
    • Xu, X. M., and Möller, S. G. (2004). AtNAP7 is a plastidic SufC-like ATP-binding cassette/ATPase essential for Arabidopsis embryogenesis. Proc. Natl. Acad. Sci. U.S.A.101, 9143-9148. doi: 10.1073/pnas.0400799101
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 9143-9148
    • Xu, X.M.1    Möller, S.G.2
  • 97
    • 70350350951 scopus 로고    scopus 로고
    • The construction of maize root cDNA library induced under iron deficiency and screening and identification of iron stress gene (fdr3)
    • Yin, L. P., Qi, X. P., and Liu, X. L. (2000). The construction of maize root cDNA library induced under iron deficiency and screening and identification of iron stress gene (fdr3). Beijing Sci. Press 45, 44-48.
    • (2000) Beijing Sci. Press , vol.45 , pp. 44-48
    • Yin, L.P.1    Qi, X.P.2    Liu, X.L.3
  • 98
    • 77956634838 scopus 로고    scopus 로고
    • Porins in prokaryotes and eukaryotes: Common themes and variations
    • Zeth, K., and Thein, M. (2010). Porins in prokaryotes and eukaryotes: common themes and variations. Biochem. J. 431, 13-22. doi: 10.1042/BJ20100371
    • (2010) Biochem. J. , vol.431 , pp. 13-22
    • Zeth, K.1    Thein, M.2
  • 99
    • 34247220295 scopus 로고    scopus 로고
    • Iron deficiency differently affects metabolic responses in soybean roots
    • Zocchi, G., De Nisi, P., Dell'Orto, M., Espen, L., and Gallina, P. M. (2007). Iron deficiency differently affects metabolic responses in soybean roots. J. Exp. Bot. 58, 993-1000. doi: 10.1093/jxb/erl259
    • (2007) J. Exp. Bot. , vol.58 , pp. 993-1000
    • Zocchi, G.1    De Nisi, P.2    Dell'Orto, M.3    Espen, L.4    Gallina, P.M.5
  • 100
    • 80051994547 scopus 로고    scopus 로고
    • Facile transfer of [2Fe-2S] clusters from the diabetes drug target mitoNEET to an apo-acceptor protein
    • Zuris, J. A., Harir, Y., Conlan, A. R., Shvartsman, M., Michaeli, D., Tamir, S., et al. (2011). Facile transfer of [2Fe-2S] clusters from the diabetes drug target mitoNEET to an apo-acceptor protein. Proc. Natl. Acad. Sci. U.S.A. 108, 13047-13052. doi: 10.1073/pnas.1109986108
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 13047-13052
    • Zuris, J.A.1    Harir, Y.2    Conlan, A.R.3    Shvartsman, M.4    Michaeli, D.5    Tamir, S.6


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