Abstract
In germinating fatty seedlings, microbodies are differentiated to leaf peroxisomes from glyoxysomes during greening, and then transformed to glyoxysomes from leaf peroxisomes during senescence. These transformations of microbodies are regulated at various level, such as gene expression, splicing of the mRNA and degradation of microbody proteins. In order to clarify the regulatory mechanisms underlying these transformations of microbodies, we tried to obtain glyoxysome-deficient mutants of Arabidopsis. We screened 2,4-dichlorophenoxybutyric acid (2,4-DB) mutants of Arabidopsis which have defects in glyoxysomal fatty acid β-oxidation. Four mutants can be classified as carrying alleles at three independent loci, which we designatedped1, ped2, andped3, respectively (whereped stands for peroxisome defective). The characteristics of theseped mutants are described.
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Beeching, J.R. andNorthcote, D.H. 1987. Nucleic acid (cDNA) and amino acid sequences of isocitrate lyase from castor bean. Plant Mol. Biol.8: 471–475.
Comai, L., Baden, C.S. andHarada, J.J. 1989. Deduced sequence of a malate synthase polypeptide encoded by a subclass of the gene family. J. Biol. Chem.264: 2778–2782.
De Bellis, L. andNishimura, M. 1991. Development of enzymes of the glyoxylate cycle during senescence of pumpkin cotyledons. Plant Cell Physiol.32: 555–561.
De Bellis, L., Tsugeki, R. andNishimura, M. 1991. Glyoxylate cycle enzymes in peroxisomes isolated from petals of pumpkin (Cucurbita sp.) during senescence. Plant Cell Physiol.32: 1227–1235.
Gietl, C. 1990. Glyoxysomal malate dehydrogenase from watermelon is synthesized with an amino-terminal transit peptide. Proc. Natl. Acad. Sci. USA87: 5773–5777.
Gould, S.J., Keller, G.-A.A. andSubramani, S. 1987. Identification of a peroxisomal targeting signal at the carboxy terminus of firefly luciferase. J. Cell. Biol.105: 2923–2931.
Graham, I.A., Smith, L.M., Brown, J.W., Leaver, C.J. andSmith, S.M. 1989. The malate synthase gene of cucumber. Plant Mol. Biol.13: 673–684.
Greenler, J.M., Sloan, J.S., Schwartz, B.W. andBecker, W.M. 1989. Isolation, characterization and sequence analysis of a full-length cDNA clone encoding NADH-dependent hydroxypyruvate reductase from cucumber. Plant Mol. Biol.13: 139–150.
Hayashi, H., De Bellis, L., Yamaguchi, K., Kato, A., Mano, S., Hayashi, M. andNishimura, M. 1998a. 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.
Hayashi, M., Aoki, M., Kato, A., Kondo, M. andNishimura, M. 1996a. Transport of chimeric proteins that contain a carboxy-terminal targeting signal into plant microbodies. Plant J.10: 225–234.
Hayashi, M., Aoki, M., Kondo, M. andNishimura, 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.
Hayashi, M., Toriyama, K., Kondo, M. andNishimura, M. 1998b. 2,4-Dicholorophenoxybutyric acid-resistant mutants of Arabidopsis have defects on glyoxysomal fatty acid β-oxidation. Plant Cell10: 183–195.
Hayashi, M., Tsugeki, R., Kondo, M., Mori, H. andNishimura, M. 1996b. Pumpkin hydroxypyruvate reductases with and without a putative C-terminal signal for targeting to microbodies may be produced by alternative splicing. Plant Mol. Biol.30: 183–189.
Kato, A., Hayashi, M., Kondo, M., andNishimura, M. 1996a. Targeting and processing of a chimeric protein with the N-terminal presequence of the precursor to glyoxysomal citrate synthase. Plant Cell8: 1601–1611.
Kato, A., Hayashi, M., Mori, H. andNishimura, 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.
Kato, A., Hayashi, M., Takeuchi, Y. andNishimura, M. 1996b. cDNA cloning and expression of a gene for 3-ketoacyl-CoA thiolase in pumpkin cotyledons. Plant Mol. Biol.31: 843–852.
Kato, A., Takeda-Yoshikawa, Y., Hayashi, M., Kondo, M., Hara-Nishimura, I. andNishimura, M. 1998. Glyoxysomal malate dehydrogenase in pumpkin: cloning of a cDNA and functional analysis of its prosequence. Plant Cell Physiol.39: 186–195.
Keller, G.A., Krisans, S., Gould, S.J., Sommer, J.M., Wang, C.C., Schliebs, W., Kunau, W., Brody, S. andSubramani, S. 1991. Evolutionary conservation of a microbody targeting signal that targets proteins to peroxisomes, glyoxysomes, and glycosomes. J. Cell. Biol.114: 893–904.
Mano, S., Hayashi, M., Kondo, M. andNishimura, M. 1996. cDNA cloning and expression of a gene for isocitrate lyase in pumpkin cotyledons. Plant Cell Physiol.37: 941–948.
Mori, H., Takeda-Yoshikawa, Y., Hara-Nishimura, I. andNishimura, M. 1991. Pumpkin malate synthase: Cloning and sequencing of the cDNA and Northern blot analysis. Eur. J. Biochem.197: 331–336.
Nishimura, M., Hayashi, M., Kato, A., Yamaguchi, K. andMano, S. 1996. Functional transformation of microbodies in higher plant cells. Cell Struct. Funct.21: 387–393.
Nishimura, M., Takeuchi, Y., De Bellis, L. andHara-Nishimura, I. 1993. Leaf peroxisomes are directly transformed to glyoxysomes during senescence of pumpkin cotyledons. Protoplasma175: 131–137.
Nishimura, M., Yamaguchi, J., Mori, H., Akazawa, T. andYokota, S. 1986. Immunocytochemical analysis shows that glyoxysomes are directly transformed to leaf peroxisomes during greening of pumpkin cotyledons. Plant Physiol.80: 313–316.
Preisig-Muller, R., Guhnemann-Schafer, K. andKindl, H. 1994. Domains of the tetrafunctional protein acting in glyoxysomal fatty acid beta-oxidation. Demonstration of epimerase and isomerase activities on a peptide lacking hydratase activity. J. Biol. Chem.269: 20475–20481.
Preisig-Muller, R. andKindl, H. 1993. Thiolase mRNA translatedin vitro yields a peptide with a putative N-terminal presequence. Plant Mol. Biol.22: 59–66.
Rodriguez, D., Ginger, R.S., Baker, A. andNorthcote, D.H. 1990. Nucleotide sequence analysis of a cDNA clone encoding malate synthase of castor bean (Ricinus communis) reveals homology to DAL7, a gene involved in allantoin degradation inSaccharomyces cerevisiae. Plant Mol. Biol.15: 501–504.
Titus, D.E. andBecker, W.M. 1985. Investigation of the glyoxysome-peroxisome transition in germinating cucumber cotyledons using double-label immunoelectron microscopy. J. Cell. Biol.101: 1288–1299.
Tsugeki, R., Hara-Nishimura, I., Mori, H. andNishimura, M. 1993. Cloning and sequencing of cDNA for glycolate oxidase from pumpkin cotyledons and Northern blot analysis. Plant Cell Physiol.34: 51–57.
Turley, R.B., Choe, S.M., Ni, W. andTrelease, R.N. 1990a. Nucleotide sequence of cottonseed malate synthase. Nucleic Acids Res.18: 3643.
Turley, R.B., Choe, S.M. andTrelease, R.N. 1990b. Characterization of a cDNA clone encoding the complete amino acid sequence of cotton isocitrate lyase. Biochim. Biophys. Acta1049: 223–226.
Volokita, M. andSomerville, 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.
Wain, R.L. andWightman, F. 1954. The growth-regulating activity of certain ω-substituted alkyl carboxylic acids in relation to their β-oxidation within the plant. Proc. Roy. Soc. Lond. Biol. Sci.142: 525–536.
Zhang, J.Z., Gomez, P.M., Baden, C.S. andHarada, J.J. 1993. Two classes of isocitrate lyase genes are expressed during late embryogeny and postgermination inBrassica napus L. Mol. Gen. Genet.238: 1770184.
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Nishimura, M., Hayashi, M., Toriyama, K. et al. Microbody defective mutants of arabidopsis. J. Plant Res. 111, 329–332 (1998). https://doi.org/10.1007/BF02512192
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DOI: https://doi.org/10.1007/BF02512192