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Plant and Cell Physiology, 2001, Vol. 42, No. 8 835-841
© 2001 Oxford University Press

Developmental Analysis of a Putative ATP/ADP Carrier Protein Localized on Glyoxysomal Membranes During the Peroxisome Transition in Pumpkin Cotyledons

Youichiro Fukao1,2, Yasuko Hayashi3, Shoji Mano1, Makoto Hayashi1 and Mikio Nishimura ,1,2,4

1 Departmnt of Cell Biology, National Institute for Basic Biology, Okazaki, 444-8585 Japan 2 Department of Molecular Biomechanics, School of Life Science, Graduate University for Advanced Studies, Okazaki, 444-8585 Japan 3 Departmnt of Environmental Science, Faculty of Science, Niigata University, Ikarashi, Niigata, 950-2181 Japan

In order to clarify the peroxisomal membrane proteins (PMPs), we characterized one of the major PMPs, PMP38. The deduced amino acid sequence for its cDNA in Arabidopsis thaliana contained polypeptides with 331 amino acids and had high similarity with those of Homo sapiens PMP34 and Candida boidinii PMP47 known as homologues of mitochondrial ATP/ADP carrier protein. We expected PMP38 to be localized on peroxisomal membranes, because it had the membrane peroxisomal targeting signal. Cell fractionation and immunocytochemical analysis using pumpkin cotyledons revealed that PMP38 is localized on peroxisomal membranes as an integral membrane protein. The amount of PMP38 in pumpkin cotyledons increased and reached the maximum protein level after 6 d in the dark but decreased thereafter. Illumination of the seedlings caused a significant decrease in the amount of the protein. These results clearly showed that the membrane protein PMP38 in glyoxysomes changes dramatically during the transformation of glyoxysomes to leaf peroxisomes, as do the other glyoxysomal enzymes, especially enzymes of the fatty acid ß-oxidation cycle, that are localized in the matrix of glyoxysomes.

4 Corresponding author: E-mail, mikosome@nibb.ac.jp; Fax, +81-564-55-7505.


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