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J. Biol. Chem., Vol. 268, Issue 18, 13280-13285, Jun, 1993
W Chen, HH Lim and L Lim
A Caenorhabditis elegans cDNA encoding a homologue of the p21 ras- related
CDC42, designated as CDC42Ce, was isolated from a nematode mixed stage cDNA
library. The encoded protein of 188 amino acid residues has 85% identity to
both human G25K and CDC42Hs and 79 and 76% identity to the yeast CDC42Sp
and CDC42Sc proteins, respectively. The CDC42Ce cDNA maps to a position on
C. elegans chromosome II in close proximity to lin-26, a cell lineage gene.
The CDC42Ce cDNA hybridizes to 2- and 1.5-kilobase mRNAs. Their expression
is developmentally regulated with highest levels at the embryonic stage,
decreasing progressively during development except for an increase of the
more abundant 1.5-kilobase mRNA at the L3 stage. The glutathione S-
transferase/CDC42Ce fusion protein expressed in Escherichia coli displays
both GTP binding and intrinsic GTPase activities. The GTPase activity of
CDC42Ce is moderately stimulated by human n-chimaerin, a GTPase-activating
protein for the related p21 rac1. The CDC42Ce protein complements the
temperature-sensitive lethal mutation cdc42-1 in yeast Saccharomyces
cerevisiae. These data suggest that CDC42Ce is the C. elegans homologue of
the yeast CDC42. The developmental expression pattern of mRNA and is
biochemical properties of its encoded protein which are closely related to
CErac1 suggest that the two p21s might be involved in related biological
processes.
The CDC42 homologue from Caenorhabditis elegans. Complementation of yeast mutation
Institute of Molecular and Cell Biology, National University of Singapore.
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