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Volumn 7, Issue AUG2016, 2016, Pages

Allocation of heme is differentially regulated by ferrochelatase isoforms in Arabidopsis cells

Author keywords

Biotic stress; Cytochromes; Ferrochelatase; Heme allocation; Photosynthesis; Plastid

Indexed keywords


EID: 84986564761     PISSN: None     EISSN: 1664462X     Source Type: Journal    
DOI: 10.3389/fpls.2016.01326     Document Type: Article
Times cited : (36)

References (42)
  • 1
    • 23344454474 scopus 로고    scopus 로고
    • Modulation of photosynthetic electron transport in the absence of terminal electron acceptors: Characterization of the rbcL deletion mutant of tobacco
    • Allahverdiyeva, Y., Mamedov, F., Maenpaa, P., Vass, I., and Aro, E. M. (2005). Modulation of photosynthetic electron transport in the absence of terminal electron acceptors: characterization of the rbcL deletion mutant of tobacco. Biochim. Biophys. Acta 1709, 69-83. doi: 10.1016/j.bbabio.2005.06.004
    • (2005) Biochim. Biophys. Acta , vol.1709 , pp. 69-83
    • Allahverdiyeva, Y.1    Mamedov, F.2    Maenpaa, P.3    Vass, I.4    Aro, E.M.5
  • 2
    • 0001844190 scopus 로고
    • Copper enyzmes in isolated chloroplasts. Polyphenol oxidase in Beta vulgaris
    • Arnon, D. (1949). Copper enyzmes in isolated chloroplasts. Polyphenol oxidase in Beta vulgaris. Plant Physiol. 24, 1-5. doi: 10.1104/pp.24.1.1
    • (1949) Plant Physiol. , vol.24 , pp. 1-5
    • Arnon, D.1
  • 4
    • 77956044833 scopus 로고    scopus 로고
    • Ferrochelatase forms an oligomeric complex with mitoferrin-1 and Abcb10 for erythroid heme biosynthesis
    • Chen, W., Dailey, H. A., and Paw, B. H. (2010). Ferrochelatase forms an oligomeric complex with mitoferrin-1 and Abcb10 for erythroid heme biosynthesis. Blood 116, 628-630. doi: 10.1182/blood-2009-12-259614
    • (2010) Blood , vol.116 , pp. 628-630
    • Chen, W.1    Dailey, H.A.2    Paw, B.H.3
  • 5
    • 0000624972 scopus 로고    scopus 로고
    • Two different genes encode ferrochelatase in Arabidopsis: Mapping, expression and subcellular targeting of the precursor proteins
    • Chow, K. S., Singh, D. P., Walker, A. R., and Smith, A. G. (1998). Two different genes encode ferrochelatase in Arabidopsis: mapping, expression and subcellular targeting of the precursor proteins. Plant J. 15, 531-541. doi: 10.1046/j.1365-313X.1998.00235.x
    • (1998) Plant J. , vol.15 , pp. 531-541
    • Chow, K.S.1    Singh, D.P.2    Walker, A.R.3    Smith, A.G.4
  • 6
    • 77955081062 scopus 로고    scopus 로고
    • Taxonomic distribution and origins of the extended LHC (light-harvesting complex) antenna protein superfamily
    • Engelken, J., Brinkmann, H., and Adamska, I. (2010). Taxonomic distribution and origins of the extended LHC (light-harvesting complex) antenna protein superfamily. BMC Evol. Biol. 10: 233. doi: 10.1186/1471-2148-10-233
    • (2010) BMC Evol. Biol. , vol.10 , pp. 233
    • Engelken, J.1    Brinkmann, H.2    Adamska, I.3
  • 7
    • 84863936201 scopus 로고    scopus 로고
    • Evaluation of unbound free heme in plant cells by differential acetone extraction
    • Espinas, N. A., Kobayashi, K., Takahashi, S., Mochizuki, N., and Masuda, T. (2012). Evaluation of unbound free heme in plant cells by differential acetone extraction. Plant Cell Physiol. 53, 1344-1354. doi: 10.1093/pcp/pcs067
    • (2012) Plant Cell Physiol. , vol.53 , pp. 1344-1354
    • Espinas, N.A.1    Kobayashi, K.2    Takahashi, S.3    Mochizuki, N.4    Masuda, T.5
  • 8
    • 0025897315 scopus 로고
    • Chlorophyll a/bbinding proteins: An extended family
    • Green, B. R., Pichersky, E., and Kloppstech, K. (1991). Chlorophyll a/bbinding proteins: an extended family. Trends Biochem. Sci. 16, 181-186. doi: 10.1016/0968-0004(91)90072-4
    • (1991) Trends Biochem. Sci. , vol.16 , pp. 181-186
    • Green, B.R.1    Pichersky, E.2    Kloppstech, K.3
  • 9
    • 84867549004 scopus 로고    scopus 로고
    • Disrupting the bimolecular binding of the heme binding protein 5 (AtHBP5) with heme oxygenase I (HYI) leads to oxidative stress in Arabidopsis
    • Hye-Jung, L., Masuda, T., and Buckhout, T. J. (2012). Disrupting the bimolecular binding of the heme binding protein 5 (AtHBP5) with heme oxygenase I (HYI) leads to oxidative stress in Arabidopsis. J. Exp. Bot. 63, 5967-5978. doi: 10.1093/jxb/errs321432
    • (2012) J. Exp. Bot. , vol.63 , pp. 5967-5978
    • Hye-Jung, L.1    Masuda, T.2    Buckhout, T.J.3
  • 10
    • 0033012091 scopus 로고    scopus 로고
    • A guide to the Lhc genes and their relatives in Arabidopsis
    • Jansson, S. (1999). A guide to the Lhc genes and their relatives in Arabidopsis. Trends Plant Sci. 4, 236-240. doi: 10.1016/S1360-1385(99) 01419-3
    • (1999) Trends Plant Sci. , vol.4 , pp. 236-240
    • Jansson, S.1
  • 11
    • 84881416216 scopus 로고    scopus 로고
    • Photosynthesis of root chloroplasts developed in Arabidopsis lines overexpressing GOLDEN2-LIKE transcription factors
    • Kobayashi, K., Sasaki, D., Noguchi, K., Fujinuma, D., Komatsu, H., Kobayashi, M., et al. (2013). Photosynthesis of root chloroplasts developed in Arabidopsis lines overexpressing GOLDEN2-LIKE transcription factors. Plant Cell Physiol. 54, 1365-1377. doi: 10.1093/pcp/pct086
    • (2013) Plant Cell Physiol. , vol.54 , pp. 1365-1377
    • Kobayashi, K.1    Sasaki, D.2    Noguchi, K.3    Fujinuma, D.4    Komatsu, H.5    Kobayashi, M.6
  • 12
    • 1542378925 scopus 로고    scopus 로고
    • New fluorescence parameters for the determination of q(a) redox state and excitation energy fluxes
    • Kramer, D. M., Johnson, G., Kiirats, O., and Edwards, G. E. (2004). New fluorescence parameters for the determination of q(a) redox state and excitation energy fluxes. Photosyn. Res. 79, 209-218. doi: 10.1023/B: PRES.0000015391.99477.0d
    • (2004) Photosyn. Res. , vol.79 , pp. 209-218
    • Kramer, D.M.1    Johnson, G.2    Kiirats, O.3    Edwards, G.E.4
  • 13
    • 0042853494 scopus 로고    scopus 로고
    • Subcellular localization of two types of ferrochelatase in cucumber
    • Masuda, T., Suzuki, T., Shimada, H., Ohta, H., and Takamiya, K. (2003). Subcellular localization of two types of ferrochelatase in cucumber. Planta 217, 602-609. doi: 10.1007/s00425-003-1019-2
    • (2003) Planta , vol.217 , pp. 602-609
    • Masuda, T.1    Suzuki, T.2    Shimada, H.3    Ohta, H.4    Takamiya, K.5
  • 14
    • 33746272007 scopus 로고    scopus 로고
    • Chemiluminescent-based method for heme determination by reconstitution with horseradish peroxidase apo-enzyme
    • Masuda, T., and Takahashi, S. (2006). Chemiluminescent-based method for heme determination by reconstitution with horseradish peroxidase apo-enzyme. Anal. Biochem. 355, 307-309. doi: 10.1016/j.ab.2006.04.008
    • (2006) Anal. Biochem. , vol.355 , pp. 307-309
    • Masuda, T.1    Takahashi, S.2
  • 15
    • 0034063592 scopus 로고    scopus 로고
    • Chlorophyll fluorescence - E practical guide
    • Maxwell, K., and Johnson, G. N. (2000). Chlorophyll fluorescence - a practical guide. J. Exp. Bot. 51, 659-668. doi: 10.1093/jexbot/51.345.659
    • (2000) J. Exp. Bot. , vol.51 , pp. 659-668
    • Maxwell, K.1    Johnson, G.N.2
  • 16
    • 84989675168 scopus 로고
    • Light-absorption and electron-transport balance between photosystem II and photosystem I in spinach chloroplasts
    • Melis, A., Spangfort, M., and Andersson, B. (1987). Light-absorption and electron-transport balance between photosystem II and photosystem I in spinach chloroplasts. Photochem. Photobiol. 45, 129-136. doi: 10.1111/j.1751-1097.1987.tb08413.x
    • (1987) Photochem. Photobiol. , vol.45 , pp. 129-136
    • Melis, A.1    Spangfort, M.2    Andersson, B.3
  • 18
    • 84982358134 scopus 로고
    • A revised medium for rapid growth and bioassays with tobacco tissue cultures
    • Murashige, T., and Skoog, F. (1962). A revised medium for rapid growth and bioassays with tobacco tissue cultures. Physiol. Plant. 15, 473-497. doi: 10.1111/j.1399-3054.1962.tb08052.x
    • (1962) Physiol. Plant. , vol.15 , pp. 473-497
    • Murashige, T.1    Skoog, F.2
  • 19
    • 78650986196 scopus 로고    scopus 로고
    • Manipulation of photoprotection to improve plant photosynthesis
    • Murchie, E. H., and Niyogi, K. K. (2011). Manipulation of photoprotection to improve plant photosynthesis. Plant Physiol. 155, 86-92. doi: 10.1104/pp.110.168831
    • (2011) Plant Physiol. , vol.155 , pp. 86-92
    • Murchie, E.H.1    Niyogi, K.K.2
  • 20
    • 0030909520 scopus 로고    scopus 로고
    • Structure and distribution of lignin in primary and secondary cell walls of maize coleoptiles analyzed by chemical and immunological probes
    • Müsel, G., Schindler, T., Bergfeld, R., Ruel, K., Jacquet, G., Lapierre, C., et al. (1997). Structure and distribution of lignin in primary and secondary cell walls of maize coleoptiles analyzed by chemical and immunological probes. Planta 201, 146-159. doi: 10.1007/Bf01007699
    • (1997) Planta , vol.201 , pp. 146-159
    • Müsel, G.1    Schindler, T.2    Bergfeld, R.3    Ruel, K.4    Jacquet, G.5    Lapierre, C.6
  • 21
    • 34250612253 scopus 로고    scopus 로고
    • Induction of isoforms of tetrapyrrole biosynthetic enzymes, AtHEMA2 and AtFC1, under stress conditions and their physiological functions in Arabidopsis
    • Nagai, S., Koide, M., Takahashi, S., Kikuta, A., Aono, M., Sasaki-Sekimoto, Y., et al. (2007). Induction of isoforms of tetrapyrrole biosynthetic enzymes, AtHEMA2 and AtFC1, under stress conditions and their physiological functions in Arabidopsis. Plant Physiol. 144, 1039-1051. doi: 10.1104/pp.107.100065
    • (2007) Plant Physiol. , vol.144 , pp. 1039-1051
    • Nagai, S.1    Koide, M.2    Takahashi, S.3    Kikuta, A.4    Aono, M.5    Sasaki-Sekimoto, Y.6
  • 22
    • 84877654048 scopus 로고    scopus 로고
    • Photosystem II assembly: From cyanobacteria to plants
    • Nickelsen, J., and Rengstl, B. (2013). Photosystem II assembly: from cyanobacteria to plants. Annu. Rev. Plant Biol. 64, 609-635. doi: 10.1146/annurev-arplant-050312-120124
    • (2013) Annu. Rev. Plant Biol. , vol.64 , pp. 609-635
    • Nickelsen, J.1    Rengstl, B.2
  • 23
    • 84866985208 scopus 로고    scopus 로고
    • A missense mutation in the glucosamine-6-phosphate N-acetyltransferaseencoding gene causes temperature-dependent growth defects and ectopic lignin deposition in Arabidopsis
    • Nozaki, M., Sugiyama, M., Duan, J., Uematsu, H., Genda, T., and Sato, Y. (2012). A missense mutation in the glucosamine-6-phosphate N-acetyltransferaseencoding gene causes temperature-dependent growth defects and ectopic lignin deposition in Arabidopsis. Plant Cell 24, 3366-3379. doi: 10.1105/tpc.112.102806
    • (2012) Plant Cell , vol.24 , pp. 3366-3379
    • Nozaki, M.1    Sugiyama, M.2    Duan, J.3    Uematsu, H.4    Genda, T.5    Sato, Y.6
  • 24
    • 84964310811 scopus 로고    scopus 로고
    • Functional update of the auxiliary proteins PsbW, PsbY, HCF136, PsbN, TerC and ALB3 in maintenance and assembly of PSII
    • Plochinger, M., Schwenkert, S., von Sydow, L., Schroder, W. P., and Meurer, J. (2016). Functional update of the auxiliary proteins PsbW, PsbY, HCF136, PsbN, TerC and ALB3 in maintenance and assembly of PSII. Front. Plant Sci. 7: 423. doi: 10.3389/fpls.2016.00423
    • (2016) Front. Plant Sci. , vol.7 , pp. 423
    • Plochinger, M.1    Schwenkert, S.2    von Sydow, L.3    Schroder, W.P.4    Meurer, J.5
  • 25
    • 0000711907 scopus 로고
    • Interrelationship between lignin deposition and the activities of peroxidase isoenzymes in differentiating tracheary elements of Zinnia: Analysis using L-α-aminooxy-β-phenylpropionic acid and 2-aminoindan-2-phosphonic acid
    • Sato, Y., Sugiyama, M., Górecki, R. J., Fukuda, H., and Komamine, A. (1993). Interrelationship between lignin deposition and the activities of peroxidase isoenzymes in differentiating tracheary elements of Zinnia: analysis using L-α-aminooxy-β-phenylpropionic acid and 2-aminoindan-2-phosphonic acid. Planta 189, 584-589. doi: 10.1007/BF00198223
    • (1993) Planta , vol.189 , pp. 584-589
    • Sato, Y.1    Sugiyama, M.2    Górecki, R.J.3    Fukuda, H.4    Komamine, A.5
  • 26
    • 78650474946 scopus 로고    scopus 로고
    • Comparison between tracheary element lignin formation and extracellular lignin-like substance formation during the culture of isolated Zinnia elegans mesophyll cells
    • Sato, Y., Yajima, Y., Tokunaga, N., and Whetten, R. (2011). Comparison between tracheary element lignin formation and extracellular lignin-like substance formation during the culture of isolated Zinnia elegans mesophyll cells. Biologia 66, 88-95. doi: 10.2478/s11756-010-0130-7
    • (2011) Biologia , vol.66 , pp. 88-95
    • Sato, Y.1    Yajima, Y.2    Tokunaga, N.3    Whetten, R.4
  • 28
    • 80053635199 scopus 로고    scopus 로고
    • Crosstalk between abiotic ultraviolet-B stress and biotic (flg22) stress signalling in Arabidopsis prevents flavonol accumulation in favor of pathogen defence compound production
    • Schenke, D., Bottcher, C., and Scheel, D. (2011). Crosstalk between abiotic ultraviolet-B stress and biotic (flg22) stress signalling in Arabidopsis prevents flavonol accumulation in favor of pathogen defence compound production. Plant Cell Environ. 34, 1849-1864. doi: 10.1111/j.1365-3040.2011.02381.x
    • (2011) Plant Cell Environ. , vol.34 , pp. 1849-1864
    • Schenke, D.1    Bottcher, C.2    Scheel, D.3
  • 29
    • 0036836930 scopus 로고    scopus 로고
    • Expression analysis of the two ferrochelatase genes in Arabidopsis in different tissues and under stress conditions reveals their different roles in haem biosynthesis
    • Singh, D. P., Cornah, J. E., Hadingham, S., and Smith, A. G. (2002). Expression analysis of the two ferrochelatase genes in Arabidopsis in different tissues and under stress conditions reveals their different roles in haem biosynthesis. Plant Mol. Biol. 50, 773-788. doi: 10.1023/A: 1019959224271
    • (2002) Plant Mol. Biol. , vol.50 , pp. 773-788
    • Singh, D.P.1    Cornah, J.E.2    Hadingham, S.3    Smith, A.G.4
  • 30
    • 79953712614 scopus 로고    scopus 로고
    • Functional assignments for the C-terminal domains of the ferrochelatase from synechocystis PCC 6803: The CAB domain plays a regulatory role and region II is essential for catalysis
    • Sobotka, R., Tichy, M.,Wilde, A., and Hunter, C.N. (2010). Functional assignments for the C-terminal domains of the ferrochelatase from synechocystis PCC 6803: the CAB domain plays a regulatory role and region II is essential for catalysis. Plant Physiol. 155, 1735-1747. doi: 10.1104/pp.110.167528
    • (2010) Plant Physiol. , vol.155 , pp. 1735-1747
    • Sobotka, R.1    Tichy, M.2    Wilde, A.3    Hunter, C.N.4
  • 31
    • 0032487201 scopus 로고    scopus 로고
    • Cytochrome b559 of photosystem II
    • Stewart, D. H., and Brudvig, G. W. (1998). Cytochrome b559 of photosystem II. Biochim. Biophys. Acta 1367, 63-87. doi: 10.1016/S0005-2728(98)00139-X
    • (1998) Biochim. Biophys. Acta , vol.1367 , pp. 63-87
    • Stewart, D.H.1    Brudvig, G.W.2
  • 32
    • 0037085273 scopus 로고    scopus 로고
    • Two types of ferrochelatase in photosynthetic and nonphotosynthetic tissues of cucumber: Their difference in phylogeny, gene expression, and localization
    • Suzuki, T., Masuda, T., Singh, D. P., Tan, F. C., Tsuchiya, T., Shimada, H., et al. (2002). Two types of ferrochelatase in photosynthetic and nonphotosynthetic tissues of cucumber: their difference in phylogeny, gene expression, and localization. J. Biol. Chem. 277, 4731-4737. doi: 10.1074/jbc.M105613200
    • (2002) J. Biol. Chem. , vol.277 , pp. 4731-4737
    • Suzuki, T.1    Masuda, T.2    Singh, D.P.3    Tan, F.C.4    Tsuchiya, T.5    Shimada, H.6
  • 33
    • 84891916294 scopus 로고    scopus 로고
    • Functional analysis of light-harvesting-like protein 3 (LIL3) and its light-harvesting chlorophyll-binding motif in Arabidopsis
    • Takahashi, K., Takabayashi, A., Tanaka, A., and Tanaka, R. (2014). Functional analysis of light-harvesting-like protein 3 (LIL3) and its light-harvesting chlorophyll-binding motif in Arabidopsis. J. Biol. Chem. 289, 987-999. doi: 10.1074/jbc.M113.525428
    • (2014) J. Biol. Chem. , vol.289 , pp. 987-999
    • Takahashi, K.1    Takabayashi, A.2    Tanaka, A.3    Tanaka, R.4
  • 34
    • 66849129357 scopus 로고    scopus 로고
    • High throughput heme assay by detection of chemiluminescence of reconstituted horseradish peroxidase
    • Takahashi, S., and Masuda, T. (2009). High throughput heme assay by detection of chemiluminescence of reconstituted horseradish peroxidase. Comb. Chem. High Throughput Screen. 12, 532-535. doi: 10.2174/138620709788489028
    • (2009) Comb. Chem. High Throughput Screen. , vol.12 , pp. 532-535
    • Takahashi, S.1    Masuda, T.2
  • 35
    • 0037944100 scopus 로고    scopus 로고
    • Involvement of ABC7 in the biosynthesis of heme in erythroid cells: Interaction of ABC7 with ferrochelatase
    • Taketani, S., Kakimoto, K., Ueta, H., Masaki, R., and Furukawa, T. (2003). Involvement of ABC7 in the biosynthesis of heme in erythroid cells: interaction of ABC7 with ferrochelatase. Blood 101, 3274-3280. doi: 10.1182/blood-2002-04-1212
    • (2003) Blood , vol.101 , pp. 3274-3280
    • Taketani, S.1    Kakimoto, K.2    Ueta, H.3    Masaki, R.4    Furukawa, T.5
  • 36
    • 84860113360 scopus 로고    scopus 로고
    • Tetrapyrrole metabolism in Arabidopsis thaliana
    • Tanaka, R., Kobayashi, K., and Masuda, T. (2011). Tetrapyrrole metabolism in Arabidopsis thaliana. Arabidopsis Book 9: e0145. doi: 10.1199/tab.0145
    • (2011) Arabidopsis Book , vol.9
    • Tanaka, R.1    Kobayashi, K.2    Masuda, T.3
  • 37
    • 34249958267 scopus 로고
    • The use of chlorophyll fluorescence nomenclature in plant stress physiology
    • van Kooten, O., and Snel, J. F. (1990). The use of chlorophyll fluorescence nomenclature in plant stress physiology. Photosynth. Res. 25, 147-150. doi: 10.1007/BF00033156
    • (1990) Photosynth. Res. , vol.25 , pp. 147-150
    • van Kooten, O.1    Snel, J.F.2
  • 38
    • 79953100002 scopus 로고    scopus 로고
    • The Arabidopsis multistress regulator TSPO is a heme binding membrane protein and a potential scavenger of porphyrins via an autophagy-dependent degradation mechanism
    • Vanhee, C., Zapotoczny, G., Masquelier, D., Ghislain, M., and Batoko, H. (2011). The Arabidopsis multistress regulator TSPO is a heme binding membrane protein and a potential scavenger of porphyrins via an autophagy-dependent degradation mechanism. Plant Cell 23, 785-805. doi: 10.1105/tpc.110. 081570
    • (2011) Plant Cell , vol.23 , pp. 785-805
    • Vanhee, C.1    Zapotoczny, G.2    Masquelier, D.3    Ghislain, M.4    Batoko, H.5
  • 40
    • 84944719349 scopus 로고    scopus 로고
    • Ubiquitin facilitates a quality-control pathway that removes damaged chloroplasts
    • Woodson, J. D., Joens, M. S., Sinson, A. B., Gilkerson, J., Salome, P. A., Weigel, D., et al. (2015). Ubiquitin facilitates a quality-control pathway that removes damaged chloroplasts. Science 350, 450-454. doi: 10.1126/science.aac7444
    • (2015) Science , vol.350 , pp. 450-454
    • Woodson, J.D.1    Joens, M.S.2    Sinson, A.B.3    Gilkerson, J.4    Salome, P.A.5    Weigel, D.6
  • 41
    • 79957526624 scopus 로고    scopus 로고
    • Heme synthesis by plastid ferrochelatase I regulates nuclear gene expression in plants
    • Woodson, J. D., Perez-Ruiz, J. M., and Chory, J. (2011). Heme synthesis by plastid ferrochelatase I regulates nuclear gene expression in plants. Cur. Biol. 21, 897-903. doi: 10.1016/j.cub.2011.04.004
    • (2011) Cur. Biol. , vol.21 , pp. 897-903
    • Woodson, J.D.1    Perez-Ruiz, J.M.2    Chory, J.3
  • 42
    • 33847001993 scopus 로고    scopus 로고
    • Localization of the small CAB-like proteins in photosystem II
    • Yao, D., Kieselbach, T., Komenda, J., Promnares, K., Prieto, M. A. H., Tichy, M., et al. (2007). Localization of the small CAB-like proteins in photosystem II. J. Bio. Chem. 282, 267-276. doi: 10.1074/jbc.M605463200
    • (2007) J. Bio. Chem. , vol.282 , pp. 267-276
    • Yao, D.1    Kieselbach, T.2    Komenda, J.3    Promnares, K.4    Prieto, M.A.H.5    Tichy, M.6


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