LIM homeodomain (LIM-HD) and nuclear LIM-only proteins play important roles
in a variety of developmental processes in animals. In some cases their ac
tivities are modulated by a nuclear LIM binding protein family called Ldb/N
LI/Clim. Here we characterize the Ldb/NLI/Clim orthologue ldb-1 of the nema
tode Caenorhabditis elegans. Two alternatively spliced variants exist, whic
h differ in their amino-termini. The ldb-1 orthologue of Caenorhabditis bri
ggsae has the same structure as that of C. elegans and is highly conserved
throughout the open reading frame, while conservation to ny and vertebrate
proteins is restricted to specific domains: the dimerization domain, the nu
clear localization sequence, and the LIM interaction domain. C. elegans ldb
-1 is expressed in neurogenic tissues in embryos, in all neurons in larval
and adult stages, and in vulval cells, gonadal sheath cells, and some body
muscle cells. C. elegans LDB-1 is able to specifically bind LIM domains in
yeast two-hybrid assays. RNA inactivation studies suggest that C. elegans l
db-1 is not required for the differentiation of neurons that express the re
spective LIM-HD genes or for LIM-HD gene autoregulation. In contrast, ldb-1
is necessary for several neuronal functions mediated by LIM-HD proteins, i
ncluding the transcriptional activation of mec-2 the mechanosensory neuron-
specific stomatin. (C) 2000 Academic Press.