Abstract
DNA metabolic processes such as DNA replication, recombination,
and repair are fundamentally important for the
maintenance of genome integrity and cell viability. Although
a large number of proteins involved in these pathways have
been extensively studied, many proteins still remain to be
identified. In this study, we isolated DNA-binding proteins
from Saccharomyces cerevisiae using DNA-cellulose columns.
By analyzing the proteins using mass spectrometry, an uncharacterized
protein, Cmr1/YDL156W, was identified. Cmr1
showed sequence homology to human Damaged-DNA binding
protein 2 in its C-terminal WD40 repeats. Consistent
with this finding, the purified recombinant Cmr1 protein
was found to be intrinsically associated with DNA-binding
activity and exhibited higher affinity to UV-damaged DNA
substrates. Chromatin isolation experiments revealed that
Cmr1 localized in both the chromatin and supernatant
fractions, and the level of Cmr1 in the chromatin fraction
increased when yeast cells were irradiated with UV. These
results
suggest that Cmr1 may be involved in DNA-damage
responses in yeast.
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