Abstract
SepB is an essential, conserved protein required for chromosomal DNA metabolism in Aspergillus nidulans. Homologs of SepB include yeast Ctf4p and human hAnd-1. Molecular and bioinformatic characterization of these proteins suggests that they act as molecular scaffolds. Furthermore, recent observations implicate the yeast family members in lagging-strand replication and the establishment of sister-chromatid cohesion. Here, we demonstrate that SepB functions in the A. nidulans DNA damage response. In particular, analysis of double mutants reveals that SepB is a member of the UvsCRAD51 epistasis group. In accord with this prediction, we show that UvsC RAD51 forms DNA-damage-induced nuclear foci in a manner that requires SepB function. We also provide evidence that implicates SepB in sister-chromatid cohesion, thereby suggesting that cohesion may play a role in regulating the localization and/or assembly of UvsCRAD51 complexes.
Original language | English (US) |
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Pages (from-to) | 1391-1402 |
Number of pages | 12 |
Journal | Genetics |
Volume | 169 |
Issue number | 3 |
DOIs | |
State | Published - Mar 2005 |
ASJC Scopus subject areas
- Genetics