The Drosophila RAD21 cohesin persists at the centromere region in mitosis

W D Warren, S Steffensen, E Lin, P Coelho, M L Loupart, N Cobbe, J Y Lee, M J McKay, T Orr-Weaver, M M S Heck, C E Sunkel

Research output: Contribution to journalArticlepeer-review

Abstract / Description of output

'Cohesin' is a highly conserved multiprotein complex thought to be the primary effector of sister-chromatid cohesion in all eukaryotes. Cohesin complexes in budding yeast hold sister chromatids together from S phase until anaphase, but in metazoans, cohesin proteins dissociate from chromosomes and redistribute into the whole cell volume during prophase, well before sister chromatids separate (reviewed in [1,2]). Here we address this apparent anomaly by investigating the cell-cycle dynamics of DRAD21, the Drosophila orthologue of the Xenopus XRAD21 and Saccharomyces cerevisiae Scc1p/Mcd1p cohesins [3]. Analysis of DRAD21 in S2 Drosophila tissue culture cells and live embryos expressing a DRAD21-green fluorescent protein (GFP) fusion revealed the presence of four distinct subcellular pools of DRAD21: a cytoplasmic pool; a chromosome-associated pool which dissociates from chromatin as chromosomes condense in prophase; a short-lived centrosome-associated pool present during meta phase-ana phase; and a centromere-proximal pool which remains bound to condensed chromosomes, is found along the junction of sister chromatids between kinetochores, and persists until the meta phase-anaphase transition. We conclude that in Drosophila, and possibly all metazoans, a minor pool of cohesin remains bound to centromere-proximal chromatin after prophase and maintains sister-chromatid cohesion until the meta ph ase-anaphase transition.

Original languageEnglish
Pages (from-to)1463-1466
Number of pages4
JournalCurrent Biology
Issue number22
Publication statusPublished - 16 Nov 2000


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