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Vol. 12, Issue 10, 2921-2933, October 2001
Department of Molecular, Cellular, and Developmental Biology,
Howard Hughes Medical Institution, University of Colorado, Boulder,
Colorado 80303-0347
We describe phenotypic characterization of dli-1,
the Caenorhabditis elegans homolog of cytoplasmic dynein
light intermediate chain (LIC), a subunit of the cytoplasmic dynein
motor complex. Animals homozygous for loss-of-function mutations in
dli-1 exhibit stochastic failed divisions in late larval
cell lineages, resulting in zygotic sterility. dli-1 is
required for dynein function during mitosis. Depletion of the
dli-1 gene product through RNA-mediated gene
interference (RNAi) reveals an early embryonic requirement. One-cell
dli-1(RNAi) embryos exhibit failed cell division
attempts, resulting from a variety of mitotic defects. Specifically,
pronuclear migration, centrosome separation, and centrosome association
with the male pronuclear envelope are defective in
dli-1(RNAi) embryos. Meiotic spindle formation, however,
is not affected in these embryos. DLI-1, like its vertebrate homologs,
contains a putative nucleotide-binding domain similar to those found in
the ATP-binding cassette transporter family of ATPases as well
as other nucleotide-binding and -hydrolyzing proteins. Amino acid
substitutions in a conserved lysine residue, known to be required for
nucleotide binding, confers complete rescue in a dli-1
mutant background, indicating this is not an essential domain for DLI-1 function.
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