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Volumn 1763, Issue 12, 2006, Pages 1382-1391

Arabidopsis thaliana-A model organism to study plant peroxisomes

Author keywords

Arabidopsis; Glyoxysome; Leaf peroxisome; Lipid metabolism; Photorespiration

Indexed keywords

ARABIDOPSIS; CELL FUNCTION; GENETIC ANALYSIS; GENOME; NONHUMAN; PEROXISOME; PLANT; PLANT MODEL; PRIORITY JOURNAL; REVIEW;

EID: 33845297292     PISSN: 01674889     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2006.08.014     Document Type: Review
Times cited : (70)

References (82)
  • 1
    • 0345568156 scopus 로고    scopus 로고
    • Early research on peroxisomes in plants
    • Baker A., and Graham I.A. (Eds), Kluwer Academic publishers, Dordrecht
    • Beevers H. Early research on peroxisomes in plants. In: Baker A., and Graham I.A. (Eds). Plant Peroxisomes (2002), Kluwer Academic publishers, Dordrecht 1-17
    • (2002) Plant Peroxisomes , pp. 1-17
    • Beevers, H.1
  • 2
    • 0001326091 scopus 로고
    • Glyoxysomes in higher plants
    • Beevers H. Glyoxysomes in higher plants. Ann. N.Y. Acad. Sci. 386 (1982) 243-251
    • (1982) Ann. N.Y. Acad. Sci. , vol.386 , pp. 243-251
    • Beevers, H.1
  • 3
    • 0001124810 scopus 로고
    • Microbodies in higher plants
    • Beevers H. Microbodies in higher plants. Annu. Rev. Plant Physiol. 30 (1979) 159-193
    • (1979) Annu. Rev. Plant Physiol. , vol.30 , pp. 159-193
    • Beevers, H.1
  • 6
    • 0033617449 scopus 로고    scopus 로고
    • A novel acyl-CoA oxidase that can oxidize short-chain acyl-CoA in plant peroxisomes
    • Hayashi H., De Bellis L., Ciurli A., Kondo M., Hayashi M., and Nishimura M. A novel acyl-CoA oxidase that can oxidize short-chain acyl-CoA in plant peroxisomes. J. Biol. Chem. 274 (1999) 12715-12721
    • (1999) J. Biol. Chem. , vol.274 , pp. 12715-12721
    • Hayashi, H.1    De Bellis, L.2    Ciurli, A.3    Kondo, M.4    Hayashi, M.5    Nishimura, M.6
  • 7
    • 0032478790 scopus 로고    scopus 로고
    • Molecular characterization of a glyoxysomal long chain acyl-CoA oxidase that is synthesized as a precursor of higher molecular mass in pumpkin
    • Hayashi H., DeBellis L., Yamaguchi K., Kato A., Hayashi M., and Nishimura M. Molecular characterization of a glyoxysomal long chain acyl-CoA oxidase that is synthesized as a precursor of higher molecular mass in pumpkin. J. Biol. Chem. 273 (1998) 8301-8307
    • (1998) J. Biol. Chem. , vol.273 , pp. 8301-8307
    • Hayashi, H.1    DeBellis, L.2    Yamaguchi, K.3    Kato, A.4    Hayashi, M.5    Nishimura, M.6
  • 8
    • 0032004229 scopus 로고    scopus 로고
    • 2,4-dichlorophenoxybutyric acid-resistant mutants of Arabidopsis have defects in glyoxysomal fatty acid β-oxidation
    • Hayashi M., Toriyama K., Kondo M., and Nishimura M. 2,4-dichlorophenoxybutyric acid-resistant mutants of Arabidopsis have defects in glyoxysomal fatty acid β-oxidation. Plant Cell 10 (1998) 183-195
    • (1998) Plant Cell , vol.10 , pp. 183-195
    • Hayashi, M.1    Toriyama, K.2    Kondo, M.3    Nishimura, M.4
  • 10
    • 0022395410 scopus 로고
    • Investigation of the glyoxysome-peroxisome transition in germinating cucumber cotyledons using double-label immunoelectron microscopy
    • Titus D.E., and Becker W.M. Investigation of the glyoxysome-peroxisome transition in germinating cucumber cotyledons using double-label immunoelectron microscopy. J. Cell Biol. 101 (1985) 1288-1299
    • (1985) J. Cell Biol. , vol.101 , pp. 1288-1299
    • Titus, D.E.1    Becker, W.M.2
  • 11
    • 0001661482 scopus 로고
    • Immunocytochemical analysis shows that glyoxysomes are directly transformed to leaf peroxisomes during greening of pumpkin cotyledons
    • Nishimura M., Yamaguchi J., Mori H., Akazawa T., and Yokota S. Immunocytochemical analysis shows that glyoxysomes are directly transformed to leaf peroxisomes during greening of pumpkin cotyledons. Plant Physiol. 80 (1986) 313-316
    • (1986) Plant Physiol. , vol.80 , pp. 313-316
    • Nishimura, M.1    Yamaguchi, J.2    Mori, H.3    Akazawa, T.4    Yokota, S.5
  • 12
    • 0001188298 scopus 로고
    • Leaf peroxisomes are directly transformed to glyoxysomes during senescence of pumpkin cotyledons
    • Nishimura M., Takeuchi Y., De Bellis L., and Hara-Nishimura I. Leaf peroxisomes are directly transformed to glyoxysomes during senescence of pumpkin cotyledons. Protoplasma 175 (1993) 131-137
    • (1993) Protoplasma , vol.175 , pp. 131-137
    • Nishimura, M.1    Takeuchi, Y.2    De Bellis, L.3    Hara-Nishimura, I.4
  • 13
    • 0001223184 scopus 로고
    • Glyoxylate cycle enzymes in peroxisomes isolated from petals of pumpkin (Cucurbita sp.) during senescence
    • De Bellis L., Tsugeki R., and Nishimura M. Glyoxylate cycle enzymes in peroxisomes isolated from petals of pumpkin (Cucurbita sp.) during senescence. Plant Cell Physiol. 32 (1991) 1227-1235
    • (1991) Plant Cell Physiol. , vol.32 , pp. 1227-1235
    • De Bellis, L.1    Tsugeki, R.2    Nishimura, M.3
  • 14
    • 0000002944 scopus 로고
    • Development of enzymes of the glyoxylate cycle during senescence of pumpkin cotyledons
    • De Bellis L., and Nishimura M. Development of enzymes of the glyoxylate cycle during senescence of pumpkin cotyledons. Plant Cell Physiol. 32 (1991) 555-561
    • (1991) Plant Cell Physiol. , vol.32 , pp. 555-561
    • De Bellis, L.1    Nishimura, M.2
  • 15
    • 0000996543 scopus 로고
    • Photorespiration mutants of Arabidopsis thaliana deficient in serine-glyoxylate aminotransferase activity
    • Somerville C.R., and Ogren W.L. Photorespiration mutants of Arabidopsis thaliana deficient in serine-glyoxylate aminotransferase activity. Proc. Natl. Acad. Sci. U. S. A. 77 (1980) 2684-2687
    • (1980) Proc. Natl. Acad. Sci. U. S. A. , vol.77 , pp. 2684-2687
    • Somerville, C.R.1    Ogren, W.L.2
  • 16
    • 0000044510 scopus 로고
    • Genetic modification of photorespiration
    • Somerville C.R., and Ogren W.L. Genetic modification of photorespiration. Trends Biochem Sci. 7 (1982) 171-174
    • (1982) Trends Biochem Sci. , vol.7 , pp. 171-174
    • Somerville, C.R.1    Ogren, W.L.2
  • 17
    • 0035146277 scopus 로고    scopus 로고
    • An early Arabidopsis demonstration. Resolving a few issues concerning photorespiration
    • Somerville C.R. An early Arabidopsis demonstration. Resolving a few issues concerning photorespiration. Plant Physiol. 125 (2001) 20-24
    • (2001) Plant Physiol. , vol.125 , pp. 20-24
    • Somerville, C.R.1
  • 18
    • 0035041589 scopus 로고    scopus 로고
    • Peroxisomal alanine: glyoxylate aminotransferase (AGT1) is a photorespiratory enzyme with multiple substrates in Arabidopsis thaliana
    • Liepman A.H., and Olsen L.J. Peroxisomal alanine: glyoxylate aminotransferase (AGT1) is a photorespiratory enzyme with multiple substrates in Arabidopsis thaliana. Plant J. 25 (2001) 487-498
    • (2001) Plant J. , vol.25 , pp. 487-498
    • Liepman, A.H.1    Olsen, L.J.2
  • 19
    • 0033762717 scopus 로고    scopus 로고
    • Genetic analysis of indole-3-butyric acid responses in Arabidopsis thaliana reveals four mutant classes
    • Zolman B.K., Yoder A., and Bartel B. Genetic analysis of indole-3-butyric acid responses in Arabidopsis thaliana reveals four mutant classes. Genetics 156 (2000) 1323-1337
    • (2000) Genetics , vol.156 , pp. 1323-1337
    • Zolman, B.K.1    Yoder, A.2    Bartel, B.3
  • 21
    • 0034331230 scopus 로고    scopus 로고
    • AtPex14p maintains peroxisomal functions by determining protein targeting to three kinds of plant peroxisomes
    • Hayashi M., Nito K., Toriyama-Kato K., Kondo M., Yamaya T., and Nishimura M. AtPex14p maintains peroxisomal functions by determining protein targeting to three kinds of plant peroxisomes. EMBO J. 19 (2000) 5701-5710
    • (2000) EMBO J. , vol.19 , pp. 5701-5710
    • Hayashi, M.1    Nito, K.2    Toriyama-Kato, K.3    Kondo, M.4    Yamaya, T.5    Nishimura, M.6
  • 22
    • 0035903171 scopus 로고    scopus 로고
    • chy1, an Arabidopsis mutant with impaired β-oxidation, is defective in a peroxisomal β-hydroxyisobutyryl-CoA hydrolase
    • Zolman B.K., MonroeAugustus M., Thompson B., Hawes J.W., Krukenberg K.A., Matsuda S.P.T., and Bartel B. chy1, an Arabidopsis mutant with impaired β-oxidation, is defective in a peroxisomal β-hydroxyisobutyryl-CoA hydrolase. J. Biol. Chem. 276 (2001) 31037-31046
    • (2001) J. Biol. Chem. , vol.276 , pp. 31037-31046
    • Zolman, B.K.1    MonroeAugustus, M.2    Thompson, B.3    Hawes, J.W.4    Krukenberg, K.A.5    Matsuda, S.P.T.6    Bartel, B.7
  • 23
    • 0035201037 scopus 로고    scopus 로고
    • The Arabidopsis pxa1 mutant is defective in an ATP-binding cassette transporter-like protein required for peroxisomal fatty acid beta-oxidation
    • Zolman B.K., Silva I.D., and Bartel B. The Arabidopsis pxa1 mutant is defective in an ATP-binding cassette transporter-like protein required for peroxisomal fatty acid beta-oxidation. Plant Physiol. 127 (2001) 1266-1278
    • (2001) Plant Physiol. , vol.127 , pp. 1266-1278
    • Zolman, B.K.1    Silva, I.D.2    Bartel, B.3
  • 24
    • 1242274571 scopus 로고    scopus 로고
    • An Arabidopsis indole-3-butyric acid-response mutant defective in PEROXIN6, an apparent ATPase implicated in peroxisomal function
    • Zolman B.K., and Bartel B. An Arabidopsis indole-3-butyric acid-response mutant defective in PEROXIN6, an apparent ATPase implicated in peroxisomal function. Proc. Natl. Acad. Sci. U. S. A. 101 (2004) 1786-1791
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 1786-1791
    • Zolman, B.K.1    Bartel, B.2
  • 25
    • 15544374294 scopus 로고    scopus 로고
    • Mutations in Arabidopsis acyl-CoA oxidase genes reveal distinct and overlapping roles in beta-oxidation
    • Adham A.R., Zolman B.K., Millius A., and Bartel B. Mutations in Arabidopsis acyl-CoA oxidase genes reveal distinct and overlapping roles in beta-oxidation. Plant J. 41 (2005) 859-874
    • (2005) Plant J. , vol.41 , pp. 859-874
    • Adham, A.R.1    Zolman, B.K.2    Millius, A.3    Bartel, B.4
  • 26
    • 12844279810 scopus 로고    scopus 로고
    • The Arabidopsis peroxisomal targeting signal type 2 receptor PEX7 is necessary for peroxisome function and dependent on PEX5
    • Woodward A.W., and Bartel B. The Arabidopsis peroxisomal targeting signal type 2 receptor PEX7 is necessary for peroxisome function and dependent on PEX5. Mol. Biol. Cell 16 (2005) 573-583
    • (2005) Mol. Biol. Cell , vol.16 , pp. 573-583
    • Woodward, A.W.1    Bartel, B.2
  • 27
    • 33644825185 scopus 로고    scopus 로고
    • Identification and functional characterization of Arabidopsis PEROXIN4 and the interacting protein PEROXIN22
    • Zolman B.K., Monroe-Augustus M., Silva I.D., and Bartel B. Identification and functional characterization of Arabidopsis PEROXIN4 and the interacting protein PEROXIN22. Plant Cell 17 (2005) 3422-3435
    • (2005) Plant Cell , vol.17 , pp. 3422-3435
    • Zolman, B.K.1    Monroe-Augustus, M.2    Silva, I.D.3    Bartel, B.4
  • 30
    • 0036794689 scopus 로고    scopus 로고
    • Two long-chain acyl-CoA synthetases from Arabidopsis thaliana involved in peroxisomal fatty acid beta-oxidation
    • Fulda M., Shockey J., Werber M., Wolter F.P., and Heinz E. Two long-chain acyl-CoA synthetases from Arabidopsis thaliana involved in peroxisomal fatty acid beta-oxidation. Plant J. 32 (2002) 93-103
    • (2002) Plant J. , vol.32 , pp. 93-103
    • Fulda, M.1    Shockey, J.2    Werber, M.3    Wolter, F.P.4    Heinz, E.5
  • 31
    • 20444476835 scopus 로고    scopus 로고
    • Jasmonoic acid levels are reduced in COMATOSE ATP-binding cassette transporter mutants. Implications for transport of jasmonate precursors into peroxisomes
    • Theodoulou F.L., Slocombe S.P., Footitt S., Holdsworth M., Baker A., Larson T.R., and Grahama I.A. Jasmonoic acid levels are reduced in COMATOSE ATP-binding cassette transporter mutants. Implications for transport of jasmonate precursors into peroxisomes. Plant Physiol. 137 (2005)
    • (2005) Plant Physiol. , vol.137
    • Theodoulou, F.L.1    Slocombe, S.P.2    Footitt, S.3    Holdsworth, M.4    Baker, A.5    Larson, T.R.6    Grahama, I.A.7
  • 32
    • 0034782175 scopus 로고    scopus 로고
    • Requirement for 3-ketoacyl-CoA thiolase-2 in peroxisome development, fatty acid beta-oxidation and breakdown of triacylglycerol in lipid bodies of Arabidopsis seedlings
    • Germain V., Rylott E.L., Larson T.R., Sherson S.M., Bechtold N., Carde J.P., Bryce J.H., Graham I.A., and Smith S.M. Requirement for 3-ketoacyl-CoA thiolase-2 in peroxisome development, fatty acid beta-oxidation and breakdown of triacylglycerol in lipid bodies of Arabidopsis seedlings. Plant J. 28 (2001) 1-12
    • (2001) Plant J. , vol.28 , pp. 1-12
    • Germain, V.1    Rylott, E.L.2    Larson, T.R.3    Sherson, S.M.4    Bechtold, N.5    Carde, J.P.6    Bryce, J.H.7    Graham, I.A.8    Smith, S.M.9
  • 33
    • 0034820746 scopus 로고    scopus 로고
    • Direct interaction between glyoxysomes and lipid bodies in cotyledons of the Arabidopsis thaliana ped1 mutant
    • Hayashi Y., Hayashi H., Hayashi M., Hara-Nishimura I., and Nishimura M. Direct interaction between glyoxysomes and lipid bodies in cotyledons of the Arabidopsis thaliana ped1 mutant. Protoplasma 218 (2001) 83-94
    • (2001) Protoplasma , vol.218 , pp. 83-94
    • Hayashi, Y.1    Hayashi, H.2    Hayashi, M.3    Hara-Nishimura, I.4    Nishimura, M.5
  • 34
    • 0034602157 scopus 로고    scopus 로고
    • Promoter trapping of a novel medium-chain acyl-CoA oxidase, which is induced transcriptionally during Arabidopsis seed germination
    • Eastmond P.J., Hooks M.A., Williams D., Lange P., Bechtold N., Sarrobert C., Nussaume L., and Graham I.A. Promoter trapping of a novel medium-chain acyl-CoA oxidase, which is induced transcriptionally during Arabidopsis seed germination. J. Biol. Chem. 275 (2000) 34375-34381
    • (2000) J. Biol. Chem. , vol.275 , pp. 34375-34381
    • Eastmond, P.J.1    Hooks, M.A.2    Williams, D.3    Lange, P.4    Bechtold, N.5    Sarrobert, C.6    Nussaume, L.7    Graham, I.A.8
  • 35
    • 0033213084 scopus 로고    scopus 로고
    • Long-chain acyl-CoA oxidases of Arabidopsis
    • Hooks M.A., Kellas F., and Graham I.A. Long-chain acyl-CoA oxidases of Arabidopsis. Plant J. 20 (1999) 1-13
    • (1999) Plant J. , vol.20 , pp. 1-13
    • Hooks, M.A.1    Kellas, F.2    Graham, I.A.3
  • 36
    • 0038691611 scopus 로고    scopus 로고
    • Arabidopsis mutants in short- and medium-chain acyl-CoA oxidase activities accumulate acyl-CoAs and reveal that fatty acid beta-oxidation is essential for embryo development
    • Rylott E.L., Rogers C.A., Gilday A.D., Edgell T., Larson T.R., and Graham I.A. Arabidopsis mutants in short- and medium-chain acyl-CoA oxidase activities accumulate acyl-CoAs and reveal that fatty acid beta-oxidation is essential for embryo development. J. Biol. Chem. 278 (2003) 21370-21377
    • (2003) J. Biol. Chem. , vol.278 , pp. 21370-21377
    • Rylott, E.L.1    Rogers, C.A.2    Gilday, A.D.3    Edgell, T.4    Larson, T.R.5    Graham, I.A.6
  • 37
    • 0034126739 scopus 로고    scopus 로고
    • ACX3, a novel medium-chain acyl-coenzyme A oxidase from Arabidopsis
    • Froman B.E., Edwards P.C., Bursch A.G., and Dehesh K. ACX3, a novel medium-chain acyl-coenzyme A oxidase from Arabidopsis. Plant Physiol. 123 (2000) 733-741
    • (2000) Plant Physiol. , vol.123 , pp. 733-741
    • Froman, B.E.1    Edwards, P.C.2    Bursch, A.G.3    Dehesh, K.4
  • 39
    • 0030890954 scopus 로고    scopus 로고
    • Pex14p, a peroxisomal membrane protein binding both receptors of the two PTS-dependent import pathways
    • Albertini M., Rehling P., Erdmann R., Girzalsky W., Kiel J.A.K.W., Veenhuis M., and Kunau W.H. Pex14p, a peroxisomal membrane protein binding both receptors of the two PTS-dependent import pathways. Cell 89 (1997) 83-92
    • (1997) Cell , vol.89 , pp. 83-92
    • Albertini, M.1    Rehling, P.2    Erdmann, R.3    Girzalsky, W.4    Kiel, J.A.K.W.5    Veenhuis, M.6    Kunau, W.H.7
  • 40
    • 0036013390 scopus 로고    scopus 로고
    • Direct interaction and determination of binding domains among peroxisomal import factors in Arabidopsis thaliana
    • Nito K., Hayashi M., and Nishimura M. Direct interaction and determination of binding domains among peroxisomal import factors in Arabidopsis thaliana. Plant Cell Physiol. 43 (2002) 355-366
    • (2002) Plant Cell Physiol. , vol.43 , pp. 355-366
    • Nito, K.1    Hayashi, M.2    Nishimura, M.3
  • 41
    • 0034647937 scopus 로고    scopus 로고
    • The mammalian peroxin Pex5pL, the longer isoform of the mobile peroxisome targeting signal (PTS) type 1 transporter, translocates the Pex7p center dot PTS2 protein complex into peroxisomes via its initial docking site, Pex14p
    • Otera H., Harano T., Honsho M., Ghaedi K., Mukai S., Tanaka A., Kawai A., Shimizu N., and Fujiki Y. The mammalian peroxin Pex5pL, the longer isoform of the mobile peroxisome targeting signal (PTS) type 1 transporter, translocates the Pex7p center dot PTS2 protein complex into peroxisomes via its initial docking site, Pex14p. J. Biol. Chem. 275 (2000) 21703-21714
    • (2000) J. Biol. Chem. , vol.275 , pp. 21703-21714
    • Otera, H.1    Harano, T.2    Honsho, M.3    Ghaedi, K.4    Mukai, S.5    Tanaka, A.6    Kawai, A.7    Shimizu, N.8    Fujiki, Y.9
  • 42
    • 33645914783 scopus 로고    scopus 로고
    • Plant peroxisomes
    • Mano S., and Nishimura M. Plant peroxisomes. Vitam. Horm. 72 (2005) 111-154
    • (2005) Vitam. Horm. , vol.72 , pp. 111-154
    • Mano, S.1    Nishimura, M.2
  • 43
    • 0036010197 scopus 로고    scopus 로고
    • Distribution and characterization of peroxisomes in Arabidopsis by visualization with GFP: dynamic morphology and actin-dependent movement
    • Mano S., Nakamori C., Hayashi M., Kato A., Kondo M., and Nishimura M. Distribution and characterization of peroxisomes in Arabidopsis by visualization with GFP: dynamic morphology and actin-dependent movement. Plant Cell Physiol. 43 (2002) 331-341
    • (2002) Plant Cell Physiol. , vol.43 , pp. 331-341
    • Mano, S.1    Nakamori, C.2    Hayashi, M.3    Kato, A.4    Kondo, M.5    Nishimura, M.6
  • 44
    • 33746521147 scopus 로고    scopus 로고
    • The Arabidopsis pex12 and pex13 mutants are defective in both PTS1- and PTS2-dependent protein transport to peroxisomes
    • Mano S., Nakamori C., Hayashi C., Nito K., Kondo M., and Nishimura M. The Arabidopsis pex12 and pex13 mutants are defective in both PTS1- and PTS2-dependent protein transport to peroxisomes. Plant J. 47 (2006) 604-618
    • (2006) Plant J. , vol.47 , pp. 604-618
    • Mano, S.1    Nakamori, C.2    Hayashi, C.3    Nito, K.4    Kondo, M.5    Nishimura, M.6
  • 45
    • 2342539053 scopus 로고    scopus 로고
    • An Arabidopsis dynamin-related protein, DRP3A, controls both peroxisomal and mitochondrial division
    • Mano S., Nakamori C., Kondo M., Hayashi M., and Nishimura M. An Arabidopsis dynamin-related protein, DRP3A, controls both peroxisomal and mitochondrial division. Plant Cell Physiol. 38 (2004) 487-498
    • (2004) Plant Cell Physiol. , vol.38 , pp. 487-498
    • Mano, S.1    Nakamori, C.2    Kondo, M.3    Hayashi, M.4    Nishimura, M.5
  • 46
    • 0033212993 scopus 로고    scopus 로고
    • A defect in β-oxidation causes abnormal inflorescence development in Arabidopsis
    • Richmond T.A., and Bleecker A.B. A defect in β-oxidation causes abnormal inflorescence development in Arabidopsis. Plant Cell 11 (1999) 1911-1923
    • (1999) Plant Cell , vol.11 , pp. 1911-1923
    • Richmond, T.A.1    Bleecker, A.B.2
  • 47
    • 33644786913 scopus 로고    scopus 로고
    • The Arabidopsis thaliana multifunctional protein gene (MFP2) of peroxisomal β-oxidation is essential for seedling establishment
    • Rylott E.L., Eastmond P.J., Gilday A.D., Slocombe S.P., Larson T.R., Baker A., and Graham I.A. The Arabidopsis thaliana multifunctional protein gene (MFP2) of peroxisomal β-oxidation is essential for seedling establishment. Plant J. 45 (2006) 903-941
    • (2006) Plant J. , vol.45 , pp. 903-941
    • Rylott, E.L.1    Eastmond, P.J.2    Gilday, A.D.3    Slocombe, S.P.4    Larson, T.R.5    Baker, A.6    Graham, I.A.7
  • 48
    • 0343962242 scopus 로고    scopus 로고
    • The Arabidopsis DELAYED DEHISCENCE1 gene encodes an enzyme in the jasmonic acid synthesis pathway
    • Sanders P.M., Lee P.Y., Biesgen C., Boone J.D., Beals T.P., Weiler E.W., and Goldberg R.B. The Arabidopsis DELAYED DEHISCENCE1 gene encodes an enzyme in the jasmonic acid synthesis pathway. Plant Cell 12 (2000) 1041-1061
    • (2000) Plant Cell , vol.12 , pp. 1041-1061
    • Sanders, P.M.1    Lee, P.Y.2    Biesgen, C.3    Boone, J.D.4    Beals, T.P.5    Weiler, E.W.6    Goldberg, R.B.7
  • 49
    • 0034641758 scopus 로고    scopus 로고
    • The Arabidopsis male-sterile mutant, opr3, lacks the 12-oxophytodienoic acid reductase required for jasmonate synthesis
    • Stintzi A., and Browse J. The Arabidopsis male-sterile mutant, opr3, lacks the 12-oxophytodienoic acid reductase required for jasmonate synthesis. Proc. Natl. Acad. Sci. U. S. A. 97 (2000) 10625-10630
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 10625-10630
    • Stintzi, A.1    Browse, J.2
  • 50
    • 0010632418 scopus 로고    scopus 로고
    • Characterization and cDNA-microarray expression analysis of 12-oxophytodienoate reductases reveals differential roles for octadecanoid biosynthesis in the local versus the systemic wound response
    • Strassner J., Schaller F., Frick U.B., Howe G.A., Weiler E.W., Amrhein N., Macheroux P., and Schaller A. Characterization and cDNA-microarray expression analysis of 12-oxophytodienoate reductases reveals differential roles for octadecanoid biosynthesis in the local versus the systemic wound response. Plant J. 32 (2002) 585-601
    • (2002) Plant J. , vol.32 , pp. 585-601
    • Strassner, J.1    Schaller, F.2    Frick, U.B.3    Howe, G.A.4    Weiler, E.W.5    Amrhein, N.6    Macheroux, P.7    Schaller, A.8
  • 51
    • 0033537759 scopus 로고    scopus 로고
    • The pex16p homolog SSE1 and storage organelle formation in Arabidopsis seeds
    • Lin Y., Sun L., Nguyen L.V., Rachubinski R.A., and Goodman H.M. The pex16p homolog SSE1 and storage organelle formation in Arabidopsis seeds. Science 284 (1999) 328-330
    • (1999) Science , vol.284 , pp. 328-330
    • Lin, Y.1    Sun, L.2    Nguyen, L.V.3    Rachubinski, R.A.4    Goodman, H.M.5
  • 52
    • 3042530250 scopus 로고    scopus 로고
    • The peroxisome deficient Arabidopsis mutant sse1 exhibits impaired fatty acid synthesis
    • Lin Y., Cluette-Brown J.E., and Goodman H.M. The peroxisome deficient Arabidopsis mutant sse1 exhibits impaired fatty acid synthesis. Plant Physiol. 135 (2004) 814-827
    • (2004) Plant Physiol. , vol.135 , pp. 814-827
    • Lin, Y.1    Cluette-Brown, J.E.2    Goodman, H.M.3
  • 53
    • 0031007808 scopus 로고    scopus 로고
    • Enlarged peroxisomes are present in oleic acid-grown Yarrowia lipolytica overexpressing the PEX16 gene encoding an intraperoxisomal peripheral membrane peroxin
    • Eitzen G.A., Szilard R.K., and Rachubinski R.A. Enlarged peroxisomes are present in oleic acid-grown Yarrowia lipolytica overexpressing the PEX16 gene encoding an intraperoxisomal peripheral membrane peroxin. J. Cell Biol. 137 (1997) 1265-1278
    • (1997) J. Cell Biol. , vol.137 , pp. 1265-1278
    • Eitzen, G.A.1    Szilard, R.K.2    Rachubinski, R.A.3
  • 54
    • 0034491482 scopus 로고    scopus 로고
    • The COP/DET/FUS proteins-Regulators of eukaryotic growth and development
    • Schwechjeimer C., and Deng X.W. The COP/DET/FUS proteins-Regulators of eukaryotic growth and development. Semin. Cell Dev. Biol. 11 (2000) 495-503
    • (2000) Semin. Cell Dev. Biol. , vol.11 , pp. 495-503
    • Schwechjeimer, C.1    Deng, X.W.2
  • 55
    • 0037135162 scopus 로고    scopus 로고
    • A role for peroxisomes in photomorphogenesis and development of Arabidopsis
    • Hu J.P., Aguirre M., Peto C., Alonso J., Ecker J., and Chory J. A role for peroxisomes in photomorphogenesis and development of Arabidopsis. Science 297 (2002) 405-409
    • (2002) Science , vol.297 , pp. 405-409
    • Hu, J.P.1    Aguirre, M.2    Peto, C.3    Alonso, J.4    Ecker, J.5    Chory, J.6
  • 56
    • 0034696786 scopus 로고    scopus 로고
    • A missense mutation in the RING finger motif of PEX2 protein disturbs the import of peroxisome targeting signal 1 (PTS1)-containing protein but not the PTS2-containing protein
    • Huang Y., Ito R., Miura S., Hashimoto T., and Ito M. A missense mutation in the RING finger motif of PEX2 protein disturbs the import of peroxisome targeting signal 1 (PTS1)-containing protein but not the PTS2-containing protein. Biochem. Biophys. Res. Commun. 270 (2000) 717-721
    • (2000) Biochem. Biophys. Res. Commun. , vol.270 , pp. 717-721
    • Huang, Y.1    Ito, R.2    Miura, S.3    Hashimoto, T.4    Ito, M.5
  • 57
    • 0034649566 scopus 로고    scopus 로고
    • Arabidopsis Genome Initiative, Analysis of the genome sequence of the flowering plant Arabidopsis thaliana
    • Arabidopsis Genome Initiative, Analysis of the genome sequence of the flowering plant Arabidopsis thaliana. Nature 408 (2000) 796-815
    • (2000) Nature , vol.408 , pp. 796-815
  • 58
    • 0042768158 scopus 로고    scopus 로고
    • Genome-wide insertional mutagenesis of Arabidopsis thaliana
    • Alonso J.M., Stepanova A.N., Leisse T.J., et al. Genome-wide insertional mutagenesis of Arabidopsis thaliana. Science 301 (2003) 653-657
    • (2003) Science , vol.301 , pp. 653-657
    • Alonso, J.M.1    Stepanova, A.N.2    Leisse, T.J.3
  • 59
    • 1042279122 scopus 로고    scopus 로고
    • Peroxisomal Acyl-CoA synthetase activity is essential for seedling development in Arabidopsis thaliana
    • Fulda M., Schnurr J., Abbadi A., Heinz E., and Browse J. Peroxisomal Acyl-CoA synthetase activity is essential for seedling development in Arabidopsis thaliana. Plant Cell 16 (2004) 394-405
    • (2004) Plant Cell , vol.16 , pp. 394-405
    • Fulda, M.1    Schnurr, J.2    Abbadi, A.3    Heinz, E.4    Browse, J.5
  • 60
    • 0037353576 scopus 로고    scopus 로고
    • Identification of photorespiratory glutamate: glyoxylate aminotransferase (GGAT) gene in Arabidopsis
    • Igarashi D., Miwa T., Seki M., Kobayashi M., Kato T., Tabata S., Shinozaki K., and Ohsumi C. Identification of photorespiratory glutamate: glyoxylate aminotransferase (GGAT) gene in Arabidopsis. Plant J. 33 (2003) 975-987
    • (2003) Plant J. , vol.33 , pp. 975-987
    • Igarashi, D.1    Miwa, T.2    Seki, M.3    Kobayashi, M.4    Kato, T.5    Tabata, S.6    Shinozaki, K.7    Ohsumi, C.8
  • 62
    • 5644233748 scopus 로고    scopus 로고
    • Lipid utilization, gluconeogenesis and seedling growth in Arabidopsis mutants lacking the glyoxylate cycle enzyme malate synthase
    • Cornah J.E., Germain V., Ward J.L., Beale M.H., and Smith S.M. Lipid utilization, gluconeogenesis and seedling growth in Arabidopsis mutants lacking the glyoxylate cycle enzyme malate synthase. J. Biol. Chem. 279 (2004) 42916-42923
    • (2004) J. Biol. Chem. , vol.279 , pp. 42916-42923
    • Cornah, J.E.1    Germain, V.2    Ward, J.L.3    Beale, M.H.4    Smith, S.M.5
  • 63
    • 33644802667 scopus 로고    scopus 로고
    • Arabidopsis peroxisomal citrate synthase is required for fatty acid respiration and seed germination
    • Pracharoenwattana I., Cornah J.E., and Smith S.M. Arabidopsis peroxisomal citrate synthase is required for fatty acid respiration and seed germination. Plant Cell 17 (2005) 2037-2048
    • (2005) Plant Cell , vol.17 , pp. 2037-2048
    • Pracharoenwattana, I.1    Cornah, J.E.2    Smith, S.M.3
  • 64
    • 0035210089 scopus 로고    scopus 로고
    • How are peroxisomes formed? The role of the endoplasmic reticulum and peroxins
    • Mullen R.T., Flynn C.R., and Trelease R.N. How are peroxisomes formed? The role of the endoplasmic reticulum and peroxins. Trends Plant Sci. 6 (2001) 256-261
    • (2001) Trends Plant Sci. , vol.6 , pp. 256-261
    • Mullen, R.T.1    Flynn, C.R.2    Trelease, R.N.3
  • 65
    • 0011797395 scopus 로고    scopus 로고
    • PEX genes in plants and other organisms
    • Baker A., and Graham I.A. (Eds), Kluwer Academic Publishers, Dordrecht
    • Charlton W., and Lopez-Huertas E. PEX genes in plants and other organisms. In: Baker A., and Graham I.A. (Eds). Plant peroxisomes (2002), Kluwer Academic Publishers, Dordrecht 385-426
    • (2002) Plant peroxisomes , pp. 385-426
    • Charlton, W.1    Lopez-Huertas, E.2
  • 66
    • 0347683331 scopus 로고    scopus 로고
    • An Arabidopsis pex10 null mutant is embryo lethal, implicating peroxisomes in an essential role during plant embryogenesis
    • Sparkes I.A., Brandizzi F., Slocombe S.P., El-Shami M., Hawes C., and Baker A. An Arabidopsis pex10 null mutant is embryo lethal, implicating peroxisomes in an essential role during plant embryogenesis. Plant Physiol. 133 (2003) 1809-1819
    • (2003) Plant Physiol. , vol.133 , pp. 1809-1819
    • Sparkes, I.A.1    Brandizzi, F.2    Slocombe, S.P.3    El-Shami, M.4    Hawes, C.5    Baker, A.6
  • 67
    • 0041421192 scopus 로고    scopus 로고
    • AthPEX10, ariuclear gene essential for peroxisome and storage organelle formation during Arabidopsis embryogenesis
    • Schumann U., Wanner G., Veenhuis M., Schmid M., and Gietl C. AthPEX10, ariuclear gene essential for peroxisome and storage organelle formation during Arabidopsis embryogenesis. Proc. Natl. Acad. Sci. U. S. A. 100 (2003) 9626-9631
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 9626-9631
    • Schumann, U.1    Wanner, G.2    Veenhuis, M.3    Schmid, M.4    Gietl, C.5
  • 68
    • 26844479820 scopus 로고    scopus 로고
    • The Arabidopsis PEX12 gene is required for peroxisome biogenesis and is essential for development
    • Fan J.L., Quan S., Orth T., Awai C., Chory J., and Hu J.P. The Arabidopsis PEX12 gene is required for peroxisome biogenesis and is essential for development. Plant Physiol. 139 (2005) 231-239
    • (2005) Plant Physiol. , vol.139 , pp. 231-239
    • Fan, J.L.1    Quan, S.2    Orth, T.3    Awai, C.4    Chory, J.5    Hu, J.P.6
  • 70
    • 0034486520 scopus 로고    scopus 로고
    • Methods of double-stranded RNA-mediated gene inactivation in Arabidopsis and their use to define an essential gene in methionine biosynthesis
    • Levin J.Z., de Framond A.J., Tuttle A., Bauser M.W., and Heifetz P.B. Methods of double-stranded RNA-mediated gene inactivation in Arabidopsis and their use to define an essential gene in methionine biosynthesis. Plant Mol. Biol. 44 (2000) 759-775
    • (2000) Plant Mol. Biol. , vol.44 , pp. 759-775
    • Levin, J.Z.1    de Framond, A.J.2    Tuttle, A.3    Bauser, M.W.4    Heifetz, P.B.5
  • 71
    • 0034712919 scopus 로고    scopus 로고
    • Specific and heritable genetic interference by double-stranded RNA in Arabidopsis thaliana
    • Chuang C.-F., and Meyerowitz E.M. Specific and heritable genetic interference by double-stranded RNA in Arabidopsis thaliana. Proc. Natl. Acad. Sci. U. S. A. 97 (2000) 4985-4990
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 4985-4990
    • Chuang, C.-F.1    Meyerowitz, E.M.2
  • 73
    • 17644370711 scopus 로고    scopus 로고
    • Differential contribution of two peroxisomal protein receptors to the maintenance of peroxisomal functions in Arabidopsis
    • Hayashi M., Yagi M., Nito K., Kamada T., and Nishimura M. Differential contribution of two peroxisomal protein receptors to the maintenance of peroxisomal functions in Arabidopsis. J. Biol. Chem. 280 (2005) 14829-14835
    • (2005) J. Biol. Chem. , vol.280 , pp. 14829-14835
    • Hayashi, M.1    Yagi, M.2    Nito, K.3    Kamada, T.4    Nishimura, M.5
  • 74
    • 33845334732 scopus 로고    scopus 로고
    • Five Arabidopsis peroxin 11 homologs individually promote peroxisome elongation, duplication or aggregation
    • Lingard M.J., and Trelease R.N. Five Arabidopsis peroxin 11 homologs individually promote peroxisome elongation, duplication or aggregation. J. Cell Sci. 11 (2006) 961-972
    • (2006) J. Cell Sci. , vol.11 , pp. 961-972
    • Lingard, M.J.1    Trelease, R.N.2
  • 76
    • 0030210553 scopus 로고    scopus 로고
    • Transport of chimeric proteins that contain a carboxy-terminal targeting signal into plant microbodies
    • Hayashi M., Aoki M., Kato A., Kondo M., and Nishimura M. Transport of chimeric proteins that contain a carboxy-terminal targeting signal into plant microbodies. Plant J. 10 (1996) 225-234
    • (1996) Plant J. , vol.10 , pp. 225-234
    • Hayashi, M.1    Aoki, M.2    Kato, A.3    Kondo, M.4    Nishimura, M.5
  • 77
    • 0031154927 scopus 로고    scopus 로고
    • Changes in targeting efficiencies of proteins to plant microbodies caused by amino acid substitutions in the carboxy-terminal tripeptide
    • Hayashi M., Aoki M., Kondo M., and Nishimura M. Changes in targeting efficiencies of proteins to plant microbodies caused by amino acid substitutions in the carboxy-terminal tripeptide. Plant Cell Physiol. 38 (1997) 759-768
    • (1997) Plant Cell Physiol. , vol.38 , pp. 759-768
    • Hayashi, M.1    Aoki, M.2    Kondo, M.3    Nishimura, M.4
  • 78
    • 0742305479 scopus 로고    scopus 로고
    • Functional differentiation of peroxisomes revealed by expression profiles of peroxisomal genes in Arabidopsis thaliana
    • Kamada T., Nito K., Hayashi H., Mano S., Hayashi M., and Nishimura M. Functional differentiation of peroxisomes revealed by expression profiles of peroxisomal genes in Arabidopsis thaliana. Plant Cell Physiol. 44 (2003) 1275-1289
    • (2003) Plant Cell Physiol. , vol.44 , pp. 1275-1289
    • Kamada, T.1    Nito, K.2    Hayashi, H.3    Mano, S.4    Hayashi, M.5    Nishimura, M.6
  • 79
    • 3042586212 scopus 로고    scopus 로고
    • Specification of the peroxisome targeting signals type 1 and type 2 of plant peroxisomes by bioinformatics analyses
    • Reumann S. Specification of the peroxisome targeting signals type 1 and type 2 of plant peroxisomes by bioinformatics analyses. Plant Physiol. 135 (2004) 783-800
    • (2004) Plant Physiol. , vol.135 , pp. 783-800
    • Reumann, S.1
  • 80
    • 0038122825 scopus 로고    scopus 로고
    • In silico prediction of the peroxisomal proteome in fungi, plants and animals
    • Emanuelsson O., Elofsson A., von Heijne G., and Cristóbal S. In silico prediction of the peroxisomal proteome in fungi, plants and animals. J. Mol. Biol. 330 (2003) 443-456
    • (2003) J. Mol. Biol. , vol.330 , pp. 443-456
    • Emanuelsson, O.1    Elofsson, A.2    von Heijne, G.3    Cristóbal, S.4
  • 81
    • 0034838201 scopus 로고    scopus 로고
    • Developmental analysis of a putative ATP/ADP carrier protein localized on glyoxysomal membranes during the peroxisome transition in pumpkin cotyledons
    • Fukao Y., Hayashi Y., Mano M., Hayashi M., and Nishimura M. Developmental analysis of a putative ATP/ADP carrier protein localized on glyoxysomal membranes during the peroxisome transition in pumpkin cotyledons. Plant Cell Physiol. 42 (2001) 835-841
    • (2001) Plant Cell Physiol. , vol.42 , pp. 835-841
    • Fukao, Y.1    Hayashi, Y.2    Mano, M.3    Hayashi, M.4    Nishimura, M.5
  • 82
    • 0036346730 scopus 로고    scopus 로고
    • Proteomic analysis of leaf peroxisomal proteins in greening cotyledons of Arabidopsis thaliana
    • Fukao Y., Hayashi M., and Nishimura M. Proteomic analysis of leaf peroxisomal proteins in greening cotyledons of Arabidopsis thaliana. Plant Cell Physiol. 43 (2002) 689-696
    • (2002) Plant Cell Physiol. , vol.43 , pp. 689-696
    • Fukao, Y.1    Hayashi, M.2    Nishimura, M.3


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