메뉴 건너뛰기




Volumn 44, Issue 12, 2003, Pages 1275-1289

Functional Differentiation of Peroxisomes Revealed by Expression Profiles of Peroxisomal Genes in Arabidopsis thaliana

Author keywords

Arabidopsis thaliana; Glyoxysome; Leaf peroxisome; Protein targeting; Targeting signal; Transcriptome

Indexed keywords

ARABIDOPSIS PROTEIN; CELL RECEPTOR; ENZYME; GLYOXYLIC ACID; GLYOXYLIC ACID DERIVATIVE; PEROXISOMAL TARGETING SIGNAL 2 RECEPTOR; PEROXISOME TARGETING SIGNAL 1 RECEPTOR; PEROXISOME-TARGETING SIGNAL 1 RECEPTOR;

EID: 0742305479     PISSN: 00320781     EISSN: None     Source Type: Journal    
DOI: 10.1093/pcp/pcg173     Document Type: Article
Times cited : (90)

References (60)
  • 1
    • 0034016655 scopus 로고    scopus 로고
    • Evidence implicating a novel thiol methyltransferase in the detoxification of glucosinolate hydrolysis products in Brassica oleracea L.
    • Attieh, J., Kleppinger-Sparace, K.F., Nunes, C., Sparace, S.A. and Saini, H.S. (2000) Evidence implicating a novel thiol methyltransferase in the detoxification of glucosinolate hydrolysis products in Brassica oleracea L. Plant Cell Environ. 23: 165-174.
    • (2000) Plant Cell Environ. , vol.23 , pp. 165-174
    • Attieh, J.1    Kleppinger-Sparace, K.F.2    Nunes, C.3    Sparace, S.A.4    Saini, H.S.5
  • 2
    • 0001124810 scopus 로고
    • Microhodies in higher plants
    • Beevers, H. (1979) Microhodies in higher plants. Annu. Rev. Plant Physiol. 30: 159-193.
    • (1979) Annu. Rev. Plant Physiol. , vol.30 , pp. 159-193
    • Beevers, H.1
  • 3
    • 33745314723 scopus 로고
    • Ascorbate peroxidase in tea leaves: Occurrence of two isozymes and the differences in their enzymatic and molecular properties
    • Chen, G. and Asada, K. (1989) Ascorbate peroxidase in tea leaves: occurrence of two isozymes and the differences in their enzymatic and molecular properties. Plant Cell Physiol. 30: 987-998.
    • (1989) Plant Cell Physiol. , vol.30 , pp. 987-998
    • Chen, G.1    Asada, K.2
  • 4
    • 0015217892 scopus 로고
    • The activation of fatty acids in castor bean endosperm
    • Cooper, T.G. (1971) The activation of fatty acids in castor bean endosperm. J. Biol. Chem. 246: 3451-3455.
    • (1971) J. Biol. Chem. , vol.246 , pp. 3451-3455
    • Cooper, T.G.1
  • 5
    • 0035212728 scopus 로고    scopus 로고
    • Peroxisomes as a source of reactive oxygen species and nitric oxide signal molecules in plant cells
    • Corpas, F.J., Barroso, J.B. and del Río. L.A. (2001) Peroxisomes as a source of reactive oxygen species and nitric oxide signal molecules in plant cells. Trends Plant Sci. 6: 145-150.
    • (2001) Trends Plant Sci. , vol.6 , pp. 145-150
    • Corpas, F.J.1    Barroso, J.B.2    Del Río, L.A.3
  • 6
    • 0033977040 scopus 로고    scopus 로고
    • The multifunctional protein AtMFP2 is coordinately expressed with other genes of fatty acid beta-oxidation during seed germination in Arabidopsis thaliana (L.) Heynh
    • Eastmond, P.J. and Graham, I.A. (2000) The multifunctional protein AtMFP2 is coordinately expressed with other genes of fatty acid beta-oxidation during seed germination in Arabidopsis thaliana (L.) Heynh. Biochem. Soc. Trans. 28: 95-99.
    • (2000) Biochem. Soc. Trans. , vol.28 , pp. 95-99
    • Eastmond, P.J.1    Graham, I.A.2
  • 8
    • 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., Williams, D., Lange, P., Bechtold, N., Sarrobert, C., Nussaume, L. and Graham, I.A. (2000b) Promoter trapping of a novel medium-chain acyl-CoA oxidase, which is induced transcriptionally during Arabidopsis seed germination. J. Biol. Chem. 275: 34375-34381.
    • (2000) J. Biol. Chem. , vol.275 , pp. 34375-34381
    • Eastmond, P.J.1    Hooks, M.2    Williams, D.3    Lange, P.4    Bechtold, N.5    Sarrobert, C.6    Nussaume, L.7    Graham, I.A.8
  • 9
    • 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. (2000) ACX3, a novel medium-chain acyl-coenzyme A oxidase from Arabidopsis. Plant Physiol. 123: 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
  • 10
    • 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, S., Hayashi, M. and Nishimura, M. (2001) Developmental analysis of a putative ATP/ADP carrier protein localized on glyoxysomal membranes during the peroxisome transition in pumpkin cotyledons. Plant Cell Physiol. 42: 835-841.
    • (2001) Plant Cell Physiol. , vol.42 , pp. 835-841
    • Fukao, Y.1    Hayashi, Y.2    Mano, S.3    Hayashi, M.4    Nishimura, M.5
  • 11
    • 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. and Heinz, E. (2002) Two long-chain acyl-CoA synthetases from Arabidopsis thaliana involved in peroxisomal fatty acid beta-oxidation. Plant J. 32: 93-103.
    • (2002) Plant J. , vol.32 , pp. 93-103
    • Fulda, M.1    Shockey, J.2    Werber, M.3    Wolter, F.4    Heinz, E.5
  • 12
    • 0002425857 scopus 로고
    • Oxidative decarboxylation of blanehed-chain 2-oxo fatty acids by higher plant peroxisomes
    • Gerbling, H. and Gerhardt, B. (1988) Oxidative decarboxylation of blanehed-chain 2-oxo fatty acids by higher plant peroxisomes. Plant Physiol. 88: 13-15.
    • (1988) Plant Physiol. , vol.88 , pp. 13-15
    • Gerbling, H.1    Gerhardt, B.2
  • 13
    • 0001001724 scopus 로고
    • Peroxisomal degradation of branched-chain 2-oxo acids
    • Gerbling, H. and Gerhardt, B. (1989) Peroxisomal degradation of branched-chain 2-oxo acids. Plant Physiol. 91: 1387-1392.
    • (1989) Plant Physiol. , vol.91 , pp. 1387-1392
    • Gerbling, H.1    Gerhardt, B.2
  • 14
    • 0001389011 scopus 로고
    • Localization of β-oxidation enzymes in peroxisomes isolated from non fatty plant tissues
    • Gerhardt, B. (1983) Localization of β-oxidation enzymes in peroxisomes isolated from non fatty plant tissues. Planta 159: 238-246.
    • (1983) Planta , vol.159 , pp. 238-246
    • Gerhardt, B.1
  • 15
    • 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. (2001) 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: 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
  • 16
    • 0025331255 scopus 로고
    • Glyoxysomal malate dehydrogenase from watermelon is synthesized with an amino-terminal transit peptide
    • Gietl, C. (1990) Glyoxysomal malate dehydrogenase from watermelon is synthesized with an amino-terminal transit peptide. Proc. Natl Acad. Sci. USA 87: 5773-5777.
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 5773-5777
    • Gietl, C.1
  • 17
    • 0028180512 scopus 로고
    • Mutational analysis of the N-terminal lopogenic signal of watermelon glyoxysomal malate dehydrogenase using the heterologous host Hansenula polymorpha
    • Gietl, C., Faber, K.N., van der Klei, I.J. and Veenhuis, M. (1994) Mutational analysis of the N-terminal lopogenic signal of watermelon glyoxysomal malate dehydrogenase using the heterologous host Hansenula polymorpha. Proc. Natl Acad. Sci. USA 91: 3151-3155.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 3151-3155
    • Gietl, C.1    Faber, K.N.2    Van Der Klei, I.J.3    Veenhuis, M.4
  • 19
    • 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. (1999) A novel acyl-CoA oxidase that can oxidize short-chain acyl-CoA in plant peroxisomes. J. Biol. Chem. 274: 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
  • 21
    • 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., De Bellis, L., Yamaguchi, K., Kato, A., Hayashi, M. and Nishimura, M. (1998) 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: 8301-8307.
    • (1998) J. Biol. Chem. , vol.273 , pp. 8301-8307
    • Hayashi, H.1    De Bellis, L.2    Yamaguchi, K.3    Kato, A.4    Hayashi, M.5    Nishimura, M.6
  • 22
    • 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. (1996a) Transport of chimeric proteins that contain a carboxy-terminal targeting signal into plant microbodies. Plant J. 10: 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
  • 23
    • 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. (1997) Changes in targeting efficiencies of proteins to plant microbodies caused by amino acid substitutions in the carboxy-terminal tripeptide. Plant Cell Physiol. 38: 759-768.
    • (1997) Plant Cell Physiol. , vol.38 , pp. 759-768
    • Hayashi, M.1    Aoki, M.2    Kondo, M.3    Nishimura, M.4
  • 24
    • 0029310672 scopus 로고
    • Cytosolic aconitase participates in the glyoxylate cycle in etiolated pumpkin cotyledons
    • Hayashi, M., De Bellis, L., Alpi, A. and Nishimura, M. (1995) Cytosolic aconitase participates in the glyoxylate cycle in etiolated pumpkin cotyledons. Plant Cell Physiol. 36: 669-680.
    • (1995) Plant Cell Physiol. , vol.36 , pp. 669-680
    • Hayashi, M.1    De Bellis, L.2    Alpi, A.3    Nishimura, M.4
  • 25
    • 0036008342 scopus 로고    scopus 로고
    • Ped3p is a peroxisomal ATP-binding cassette transporter that might supply substrates for fatty acid beta-oxidation
    • Hayashi, M., Nito, K., Takei-Hoshi, R., Yagi, M., Kondo, M., Suenaga, A., Yamaya, T. and Nishimura, M. (2002b) Ped3p is a peroxisomal ATP-binding cassette transporter that might supply substrates for fatty acid beta-oxidation. Plant Cell Physiol. 43: 1-11.
    • (2002) Plant Cell Physiol. , vol.43 , pp. 1-11
    • Hayashi, M.1    Nito, K.2    Takei-Hoshi, R.3    Yagi, M.4    Kondo, M.5    Suenaga, A.6    Yamaya, T.7    Nishimura, M.8
  • 27
    • 0030019124 scopus 로고    scopus 로고
    • Pumpkin hydroxypyruvate reductases with and without a putative C-terminal signal for targeting to microbodies may be producing by alternative splicing
    • Hayashi, M., Tsugeki, R., Kondo, M., Mori, H. and Nishimura, M. (1996b) Pumpkin hydroxypyruvate reductases with and without a putative C-terminal signal for targeting to microbodies may be producing by alternative splicing. Plant Mol. Biol. 30: 183-189.
    • (1996) Plant Mol. Biol. , vol.30 , pp. 183-189
    • Hayashi, M.1    Tsugeki, R.2    Kondo, M.3    Mori, H.4    Nishimura, M.5
  • 28
    • 0742296043 scopus 로고    scopus 로고
    • Molecular biology, enzymology, and physiology of β-oxidation
    • Edited by Baker, A. and Graham, I.A. Kluwer Academic Publishers, London
    • Hooks, M.A. (2002) Molecular biology, enzymology, and physiology of β-oxidation. In Plant Peroxisomes. Edited by Baker, A. and Graham, I.A. pp. 19-55. Kluwer Academic Publishers, London.
    • (2002) Plant Peroxisomes , pp. 19-55
    • Hooks, M.A.1
  • 29
    • 0033213084 scopus 로고    scopus 로고
    • Long-chain acyl-CoA oxidases of Arabidopsis
    • Hooks, M.A., Kellas. F. and Graham, I.A. (1999) Long-chain acyl-CoA oxidases of Arabidopsis. Plant J. 20: 1-13.
    • (1999) Plant J. , vol.20 , pp. 1-13
    • Hooks, M.A.1    Kellas, F.2    Graham, I.A.3
  • 31
    • 0040557481 scopus 로고    scopus 로고
    • Evidence for the presence of the ascorbate-glutathione cycle in mitochondria and peroxisomes of pea leaves
    • Jimenez, A., Hernádez, J.A., del Río, L.A. and Sevilla, F. (1997) Evidence for the presence of the ascorbate-glutathione cycle in mitochondria and peroxisomes of pea leaves. Plant Physiol. 114: 275-284.
    • (1997) Plant Physiol. , vol.114 , pp. 275-284
    • Jimenez, A.1    Hernádez, J.A.2    Del Río, L.A.3    Sevilla, F.4
  • 33
    • 0034569737 scopus 로고    scopus 로고
    • Transport of peroxisomal proteins synthesized as large precursors in plants
    • Kato, A., Hayashi, M., Kondo, M. and Nishimura, M. (2000) Transport of peroxisomal proteins synthesized as large precursors in plants. Cell Biochem. Biophys. 32: 269-275.
    • (2000) Cell Biochem. Biophys. , vol.32 , pp. 269-275
    • Kato, A.1    Hayashi, M.2    Kondo, M.3    Nishimura, M.4
  • 34
    • 0029110307 scopus 로고
    • Molecular characterization of a glyoxysomal citrate synthase that is synthesized as a precursor of higher molecular mass in pumpkin
    • Kato, A., Hayashi, M., Mori, H. and Nishimura, M. (1995) Molecular characterization of a glyoxysomal citrate synthase that is synthesized as a precursor of higher molecular mass in pumpkin. Plant Mol. Biol. 27: 377-390.
    • (1995) Plant Mol. Biol. , vol.27 , pp. 377-390
    • Kato, A.1    Hayashi, M.2    Mori, H.3    Nishimura, M.4
  • 35
    • 0030199279 scopus 로고    scopus 로고
    • cDNA cloning and expression of a gene for 3-ketoaeyl-CoA thiolase in pumpkin cotyledons
    • Kato, A., Hayashi, M., Takeuchi, Y. and Nishimura, M. (1996) cDNA cloning and expression of a gene for 3-ketoaeyl-CoA thiolase in pumpkin cotyledons. Plant Mol. Biol. 31: 843-852.
    • (1996) Plant Mol. Biol. , vol.31 , pp. 843-852
    • Kato, A.1    Hayashi, M.2    Takeuchi, Y.3    Nishimura, M.4
  • 36
    • 0032005089 scopus 로고    scopus 로고
    • Glyoxysomal malate dehydrogenase in pumpkin: Cloning of a cDNA and functional analysis of its presequence
    • Kato, A., Takeda-Yoshikawa, Y., Hayashi, M., Kondo, M., Hara-Nishimura, I. and Nishimura, M. (1998) Glyoxysomal malate dehydrogenase in pumpkin: cloning of a cDNA and functional analysis of its presequence. Plant Cell Physiol 39: 186-195.
    • (1998) Plant Cell Physiol , vol.39 , pp. 186-195
    • Kato, A.1    Takeda-Yoshikawa, Y.2    Hayashi, M.3    Kondo, M.4    Hara-Nishimura, I.5    Nishimura, M.6
  • 37
    • 0027159789 scopus 로고
    • Fatty acid degradation in plant peroxisomes: Function and biosynthesis of the enzymes involved
    • Kindl, H. (1993) Fatty acid degradation in plant peroxisomes: Function and biosynthesis of the enzymes involved. Biochimie 75: 225-230.
    • (1993) Biochimie , vol.75 , pp. 225-230
    • Kindl, H.1
  • 38
    • 0001015272 scopus 로고
    • Cytosolic ascorhate peroxidase in seedling and leaves of maize
    • Koshiha, T. (1993) Cytosolic ascorhate peroxidase in seedling and leaves of maize. Plant Cell Physiol. 34: 713-721.
    • (1993) Plant Cell Physiol. , vol.34 , pp. 713-721
    • Koshiha, T.1
  • 41
    • 0035041589 scopus 로고    scopus 로고
    • Peroxisomal alanine: Glyoxylale aminotransferase (AGT1) is a photorespiratory enzyme with multiple substrates in Arabidopsis thaliana
    • Liepman, A. and Olsen, L. (2001) Peroxisomal alanine: glyoxylale aminotransferase (AGT1) is a photorespiratory enzyme with multiple substrates in Arabidopsis thaliana. Plant J. 25: 487-498.
    • (2001) Plant J. , vol.25 , pp. 487-498
    • Liepman, A.1    Olsen, L.2
  • 42
    • 0037250125 scopus 로고    scopus 로고
    • Alanine aminotransferase homologs catalyze the glutamate:glyoxylate aminotransferase reaction in peroxisomes of Arabidopsis
    • Liepman, A. and Olsen, L. (2003) Alanine aminotransferase homologs catalyze the glutamate:glyoxylate aminotransferase reaction in peroxisomes of Arabidopsis. Plant Physiol. 131: 215-227.
    • (2003) Plant Physiol. , vol.131 , pp. 215-227
    • Liepman, A.1    Olsen, L.2
  • 43
    • 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. (1999) The Pex16p homolog SSE1 and storage organelle formation in Arabidopsis seeds. Science 284: 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
  • 44
    • 0011063471 scopus 로고    scopus 로고
    • Light regulates alternative splicing of hydroxypyruvate reductase in pumpkin
    • Mano, S., Hayashi, M. and Nishimura, M. (1999) Light regulates alternative splicing of hydroxypyruvate reductase in pumpkin. Plant J. 17: 309-320.
    • (1999) Plant J. , vol.17 , pp. 309-320
    • Mano, S.1    Hayashi, M.2    Nishimura, M.3
  • 45
    • 0035210089 scopus 로고    scopus 로고
    • How are peroxisomes formed? The role of the endoplasmic reticulum and peroxins
    • Mullen, R.T., Flynn, C.R. and Trelcase, R.N. (2001) How are peroxisomes formed? The role of the endoplasmic reticulum and peroxins. Trends Plant Sci. 6: 256-261.
    • (2001) Trends Plant Sci. , vol.6 , pp. 256-261
    • Mullen, R.T.1    Flynn, C.R.2    Trelcase, R.N.3
  • 46
    • 0031277483 scopus 로고    scopus 로고
    • Diverse amino acid residues function within the type 1 peroxisomal targeting signal
    • Mullen, R.T., Lee, M.S., Flynn, C.R. and Trelease, R.N. (1997) Diverse amino acid residues function within the type 1 peroxisomal targeting signal. Plant Physiol. 15: 881-889.
    • (1997) Plant Physiol. , vol.15 , pp. 881-889
    • Mullen, R.T.1    Lee, M.S.2    Flynn, C.R.3    Trelease, R.N.4
  • 47
    • 0034617420 scopus 로고    scopus 로고
    • Primary structure and expression of peroxisomal acetylspermidine oxidase in the methylotrophic yeast Candida boidinii
    • Nishikawa, M., Hagishita, T., Yurimoto, H., Kato, N., Sakai, Y. and Hatanaka,. T. (2000) Primary structure and expression of peroxisomal acetylspermidine oxidase in the methylotrophic yeast Candida boidinii. FEBS Lett. 476: 150-154.
    • (2000) FEBS Lett. , vol.476 , pp. 150-154
    • Nishikawa, M.1    Hagishita, T.2    Yurimoto, H.3    Kato, N.4    Sakai, Y.5    Hatanaka, T.6
  • 49
    • 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. (2002) Direct interaction and determination of binding domains among peroxisomal import factors in Arabidopsis thaliana. Plant Cell Physiol. 43: 355-366.
    • (2002) Plant Cell Physiol. , vol.43 , pp. 355-366
    • Nito, K.1    Hayashi, M.2    Nishimura, M.3
  • 50
    • 0028102553 scopus 로고
    • Domains of the tetrafunctional protein acting in glyoxysomal fatty acid beta-oxidation
    • Preisig-Muller, R., Guhnemann-Schafer, K. and Kindl, H. (1994) Domains of the tetrafunctional protein acting in glyoxysomal fatty acid beta-oxidation. J. Biol. Chem. 269: 20475-20481.
    • (1994) J. Biol. Chem. , vol.269 , pp. 20475-20481
    • Preisig-Muller, R.1    Guhnemann-Schafer, K.2    Kindl, H.3
  • 51
    • 0033212993 scopus 로고    scopus 로고
    • A defect in β-oxidation causes abnormal inflorescence developed in Arabidopsis
    • Richmond, T.A. and Bleecker, A.B. (1999) A defect in β-oxidation causes abnormal inflorescence developed in Arabidopsis. Plant Cell 11: 1911-1923.
    • (1999) Plant Cell , vol.11 , pp. 1911-1923
    • Richmond, T.A.1    Bleecker, A.B.2
  • 52
    • 0029170675 scopus 로고
    • The aspartate aminotransferase gene family of Arabidopsis encodes isoenzymes localized to three distinct subcellular compartments
    • Schultz, C.J. and Coruzzi, G.M. (1995) The aspartate aminotransferase gene family of Arabidopsis encodes isoenzymes localized to three distinct subcellular compartments. Plant J. 7: 61-75.
    • (1995) Plant J. , vol.7 , pp. 61-75
    • Schultz, C.J.1    Coruzzi, G.M.2
  • 54
    • 0014409902 scopus 로고
    • Peroxisomes from spinach leaves containing enzymes related to glycolate metabolism
    • Tolbert, N.E., Oeser, A., Kisaki, T., Hageman, R.H. and Yamazaki, R.K. (1968) Peroxisomes from spinach leaves containing enzymes related to glycolate metabolism. J. Biol Chem. 243: 5179-5184.
    • (1968) J. Biol Chem. , vol.243 , pp. 5179-5184
    • Tolbert, N.E.1    Oeser, A.2    Kisaki, T.3    Hageman, R.H.4    Yamazaki, R.K.5
  • 55
    • 0027341713 scopus 로고
    • Cloning and sequencing of cDNA for glycolate oxidase from pumpkin cotyledons and Northern blot analysis
    • Tsugeki, R., Hara-Nishimura, I., Mori, H. and Nishimura, M. (1993) Cloning and sequencing of cDNA for glycolate oxidase from pumpkin cotyledons and Northern blot analysis. Plant Cell Physiol. 34: 51-57.
    • (1993) Plant Cell Physiol. , vol.34 , pp. 51-57
    • Tsugeki, R.1    Hara-Nishimura, I.2    Mori, H.3    Nishimura, M.4
  • 56
    • 0025339378 scopus 로고
    • Characterization of a cDNA clone encoding the complete amino acid sequence of cotton isocilrate lyase
    • Turley, R.B., Choe, S.M. and Trelease, R.N. (1990) Characterization of a cDNA clone encoding the complete amino acid sequence of cotton isocilrate lyase. Biochim. Biophys. Acta 1049: 223-226.
    • (1990) Biochim. Biophys. Acta , vol.1049 , pp. 223-226
    • Turley, R.B.1    Choe, S.M.2    Trelease, R.N.3
  • 57
    • 0023665350 scopus 로고
    • The primary structure of spinach glycolate oxidase deduced from the DNA sequence of a cDNA clone
    • Volokita, M. and Somerville, C.R. (1987) The primary structure of spinach glycolate oxidase deduced from the DNA sequence of a cDNA clone. J. Biol. Chem. 262: 15825-15828.
    • (1987) J. Biol. Chem. , vol.262 , pp. 15825-15828
    • Volokita, M.1    Somerville, C.R.2
  • 59
    • 0029375164 scopus 로고
    • A novel isoenzyme of ascorbate peroxidase localized on glyoxysomal and leaf peroxisomal membranes in pumpkin
    • Yamaguchi, K., Mori, H. and Nishimura, M. (1995) A novel isoenzyme of ascorbate peroxidase localized on glyoxysomal and leaf peroxisomal membranes in pumpkin. Plant Cell Physiol. 36: 1157-1162.
    • (1995) Plant Cell Physiol. , vol.36 , pp. 1157-1162
    • Yamaguchi, K.1    Mori, H.2    Nishimura, M.3
  • 60
    • 0035903171 scopus 로고    scopus 로고
    • chyI, an Arabidopsis mutant with impaired beta-oxidation, is defective in a peroxisomal beta-hydroxyisobutyryl-CoA hydrolase
    • Zolman. B., Monroe-Augustus, M., Thompson, B., Hawes, J., Krukenberg, K., Matsuda, S. and Bartel. B. (2001) chyI, an Arabidopsis mutant with impaired beta-oxidation, is defective in a peroxisomal beta-hydroxyisobutyryl-CoA hydrolase. J. Biol. Chem. 276: 31037-31046.
    • (2001) J. Biol. Chem. , vol.276 , pp. 31037-31046
    • Zolman, B.1    Monroe-Augustus, M.2    Thompson, B.3    Hawes, J.4    Krukenberg, K.5    Matsuda, S.6    Bartel, B.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.