Recent studies in yeast, Drosophila and humans have revealed the exist
ence of a highly conserved gene encoding a novel protein, Dodo, compri
sed of four modules: a WW domain, involved in protein-protein interact
ions, a peptidyl-prolyl cis-trans isomerase (PPIase) domain belonging
to a recently described third family of PPIases involved in protein fo
lding and unfolding, a nuclear localization motif and finally, a long,
surface-exposed a-helix that is likely to be involved in binding to a
cell cycle serine/threonine kinase. The genetic, molecular, biochemic
al and structural data are reviewed in the context of the potential bi
ological properties of this new protein family. (C) 1997 Elsevier Scie
nce B.V.