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THE PLANT CELL, Vol 5, Issue 8 941-952, Copyright © 1993 by American Society of Plant Biologists
Targeting of Glyoxysomal Proteins to Peroxisomes in Leaves and Roots of a Higher Plant
L. J. Olsen, W. F. Ettinger, B. Damsz, K. Matsudaira, M. A. Webb and J. J. Harada
Section of Botany, Division of Biological Sciences, University of California, Davis, California 95616
Higher plants possess several classes of peroxisomes that are present at
distinct developmental stages and serve different metabolic roles. To
investigate the cellular processes that regulate developmental transitions
of peroxisomal function, we analyzed the targeting of glyoxysomal proteins
to leaf-type and root peroxisomes. We transferred genes encoding the
glyoxysome-specific enzymes isocitrate lyase (IL) and malate synthase into
Arabidopsis plants and showed, in cell fractionation and immunogold
localization experiments, that the glyoxysomal proteins were imported into
leaf-type and root peroxisomes. We next defined the sequences that target
IL to peroxisomes and asked whether the same targeting determinant is
recognized by different classes of the organelle. By localizing deletion
and fusion derivatives of IL, we showed that the polypeptide's carboxyl
terminus is both necessary for its transport to peroxisomes and sufficient
to redirect a passenger protein from the cytosol to both glyoxysomes and
leaf-type peroxisomes. Thus, glyoxysomal proteins are transported into
several classes of peroxisomes using a common targeting determinant,
suggesting that protein import does not play a regulatory role in
determining a peroxisome's function. Rather, the specific metabolic role of
a peroxisome appears to be determined primarily by processes that regulate
the synthesis and/or stability of its constituent proteins. These processes
are specified by the differentiated state of the cells in which the
organelles are found.
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