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The yeast high mobility group protein, HMO1, facilitates DNA end‐joining
Author(s) -
Williams Alan Marc,
Grove Anne
Publication year - 2007
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.21.5.a291
Subject(s) - high mobility group , chromatin , dna ligase , dna , plasmid , biology , microbiology and biotechnology , ligation , genetics , gene
The Saccharomyces cerevisiae high mobility group (HMGB) protein, HMO1, is a chromatin‐associated protein that binds DNA without preference for a particular DNA sequence. It consists of two DNA binding domains (box A and box B) as well as a lysine‐rich C‐terminus. HMO1 has been suggested to be involved in a number of processes involving DNA binding, including the control of DNA mutagenesis. To explore HMO1's potential involvement in DNA repair, we determined whether HMO1 serves as an aid in DNA ligation of cohesive‐ended linearized plasmid (pGEM5). Results indicate that HMO1 increases the ability of T4 DNA ligase to end‐join the linearized plasmid into DNA multiplexes. Circularization of the linear plasmid was confirmed to not have taken place, as evidenced by the sensitivity of ligation products to Exonuclease III digestion. At elevated concentrations, HMO1 appears to inhibit DNA ligase from forming large ligation products. Combined with the ability of HMO1 to self‐associate in solution, these results suggest that HMO1 may participate in DNA double strand break repair by facilitating end‐joining. Research supported by the National Institute of Health through the Initiative for Maximizing Student Diversity at Louisiana State University.