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THE PLANT CELL, Vol 8, Issue 1 119-132, Copyright © 1996 by American Society of Plant Biologists
A Kinesin-like Protein, KatAp, in the Cells of Arabidopsis and Other Plants
B. Liu, R. J. Cyr and B. A. Palevitz
Department of Botany, University of Georgia, Athens, Georgia 30602
The kinesin-like proteins (KLPs) are a large family of plus- or
minus-end-directed microtubule motors important in intracellular transport,
mitosis, meiosis, and development. However, relatively little is known
about plant KLPs. We prepared an antibody against two peptides in the
microtubule binding domain of an Arabidopsis KLP (KatAp) encoded by the
KatA gene, one of a family of genes encoding KLPs whose motor domain is
located near the C terminus of the polypeptide. Such KLPs typically move
materials toward the minus end of microtubules. An immunoreactive band (Mr
of 140,000) corresponding to KatAp was demonstrated with this antibody on
immunoblots of Arabidopsis seedling extracts. During immunofluorescence
localizations, the antibody produced weak, variable staining in the
cytoplasm and nucleus of interphase Arabidopsis suspension cells but much
stronger staining of the mitotic apparatus during division. Staining was
concentrated near the midzone during metaphase and was retained there
during anaphase. The phragmoplast was also stained. Similar localization
patterns were seen in tobacco BY-2 cells. The antibody produced a single
band (Mr of 130,000) in murine brain fractions prepared according to
procedures that enrich for KLPs (binding to microtubules in the presence of
AMP-PNP but not ATP). A similar fraction from carrot suspension cells
yielded a cross-reacting polypeptide of similar apparent molecular mass.
When dividing BY-2 cells were lysed in the presence of taxol and ATP,
antibody staining moved rapidly toward the poles, supporting the presence
of a minus-end motor. Movement did not occur without ATP, with AMP-PNP, or
with ATP plus antibody. Our results indicate that the protein encoded by
KatA, KatAp, is expressed in Arabidopsis and is specifically localized to
the midzone of the mitotic apparatus and phragmoplast. A similar protein is
also present in other species.
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