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The histone H3 variant CENP‐A localizes to sites of DNA repair induced by laser microirradiation of living cells
Author(s) -
Zeitlin Sam G.,
Baker Norman M,
Wang Jean JY,
Berns Michael W,
Cleveland Don W
Publication year - 2008
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.22.1_supplement.600.3
Subject(s) - centromere , kinetochore , microbiology and biotechnology , histone , histone h3 , dna damage , mitosis , dna repair , biology , histone h2b , dna , chemistry , genetics , chromosome , gene
The conserved centromere protein A (CENP‐A) is most similar to histone H3, with a unique N‐terminal tail. CENP‐A is known to be essential for recruitment of other kinetochore proteins to mediate attachment of mitotic spindle microtubules to chromosomes. Recently, we reported that DNA damaging mechanisms influence CENP‐A binding to DNA in vitro. We now report that CENP‐A localizes to sites of DNA damage induced by a laser in interphase nuclei of living cells, along with known DNA repair markers such as 53BP1, phosphorylated H2AX, Nbs1 and Chk2. CENP‐A tagged with GFP rapidly localizes to sites of damage, while other tagged histones such as H3 and H2B do not.These observations suggest that CENP‐A may function in DNA repair as part of a non‐nucleosomal complex, in addition to its known function in kinetochore formation. SGZ was supported by the California Institute of Regenerative Medicine