Saccharomyces cerevisiae Cmr1 Protein Preferentially Binds to UV-Damaged DNA In Vitro

Do-Hee Choi; Sung-Hun Kwon; Joon-Ho Kim; Sung-Ho Bae

doi:10.1007/s12275-012-1597-4

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Saccharomyces cerevisiae Cmr1 Protein Preferentially Binds to UV-Damaged DNA In Vitro: Do-Hee Choi , Sung-Hun Kwon , Joon-Ho Kim , Sung-Ho Bae; Journal of Microbiology 2012;50(1):112-118.
DOI: https://doi.org/10.1007/s12275-012-1597-4
Published online: February 27, 2012

Department of Biological Sciences, College of Natural Science, Inha University, Incheon 402-751, Republic of Korea

Corresponding author: Sung-Ho Bae , Tel: +82-32-860-7712,

Received: 12 November 2011 • Accepted: 20 December 2011

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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.

Keywords: Cmr1;DNA-binding protein;damaged DNA binding;WD40 repeats;UV-irradiation;Saccharomyces cerevisiae

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Saccharomyces cerevisiae Cmr1 Protein Preferentially Binds to UV-Damaged DNA In Vitro

J. Microbiol. 2012;50(1):112-118. Published online February 27, 2012

DOI: https://doi.org/10.1007/s12275-012-1597-4

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