Cohesin is an evolutionarily conserved multiprotein complex required to est
ablish and maintain sister chromatid cohesion. Here, we report the cloning
and initial characterization of the Drosophila homologue of the fission yea
st rad21 cohesin subunit, called Drad21. The Drad21 coding region was local
ized to centromeric heterochromatin and encodes a 715 amino acid (aa) prote
in with 42% aa identity to vertebrate Rad21p-homologues, 25% with Scc1p/Mcd
1p (S. cerevisiae) and 28% with Rad21p (S. pombe). Sequences with similarit
y to the sites of proteolytic cleavage identified in Scc1p/Mcd1p are not ev
ident in DRAD21. Northern blot and mRNA in-situ studies show that Drad21 is
developmentally regulated, with high levels of expression in early embryog
enesis, in S-phase cells of proliferating imaginal tissues, and in the earl
y endocycling cells of the embryonic gut. (C) 2000 Elsevier Science B.V. Al
l rights reserved.