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Plant and Cell Physiology, 2001, Vol. 42, No. 1 20-27
© 2001 Oxford University Press

Pumpkin Peroxisomal Ascorbate Peroxidase is Localized on Peroxisomal Membranes and Unknown Membranous Structures

Kazumasa Nito1,2, Katsushi Yamaguchi1, Maki Kondo1, Makoto Hayashi1 and Mikio Nishimura ,1,2,3

1 Department of Cell Biology, National Institute for Basic Biology, Okazaki, 444-8585 Japan 2 Department of Molecular Biomechanics, School of Life Science, the Graduate University for Advanced Studies, Okazaki, 444-8585 Japan

To investigate the roles of peroxisomal membrane proteins in the reversible conversion of glyoxysomes to leaf peroxisomes, we characterized several membrane proteins of glyoxysomes. One of them was identified as an ascorbate peroxidase (pAPX) that is localized on glyoxysomal membranes. Its cDNA was isolated by immunoscreening. The deduced amino acid sequence encoded by the cDNA insert does not have a peroxisomal targeting signal (PTS), suggesting that pAPX is imported by one or more PTS-independent pathways. Subcellular fractionation of 3- and 5-d-old cotyledons of pumpkin revealed that pAPX was localized not only in the glyoxysomal fraction, but also in the ER fraction. A magnesium shift experiment showed that the density of pAPX in the ER fraction did not increase in the presence of Mg2+, indicating that pAPX is not localized in the rough ER. Immunocytochemical analysis using a transgenic Arabidopsis which expressed pumpkin pAPX showed that pAPX was localized on peroxisomal membranes, and also on a unknown membranous structure in green cotyledons. The overall results suggested that pAPX is transported to glyoxysomal membranes via this unknown membranous structure.

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


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