Data from: Evidence of centromeric histone 3 chaperone involved in DNA damage repair pathway in budding yeast

The centromeric protein-A (CENP-A) is an evolutionary conserved histone H3
variant that marks the identity of the centromeres. Several mechanisms
regulate the centromeric deposition of CENP-A as its mislocalization
causes erroneous chromosome segregation, leading to aneuploidy-based
diseases, including cancers. The most crucial deposition factor is a
CENP-A specific chaperone, HJURP (Scm3 in budding yeast), which
specifically binds to CENP-A. However, the discovery of HJURP as a DDR
(DNA damage repair) protein and evidence of its binding to Holliday
junctions in vitro indicate a CENP-A-deposition-independent role of these
chaperones. In this study, using budding yeast, we demonstrate that Scm3
is crucial for the DDR pathway as scm3 cells are sensitive to DNA damage.
We further observe that the scm3 mutant genetically interacts with the
rad52 DDR mutant and is compromised in activating DDR-mediated arrest. We
demonstrate that Scm3 associates with the DNA damage sites and undergoes
posttranslational modifications upon DNA damage. Overall, from this report
and earlier studies on HJURP, we conclude that DDR functions of CENP-A
chaperones are conserved across eukaryotes. Thus, the revelation that
these chaperones confer genome stability in more than one pathway has
clinical significance.