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A more recent version of this article appeared on February 1, 2003
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Submitted on November 14, 2001
Revised on October 15, 2002
Accepted on October 31, 2002
1 Los Alamos National Laboratory, Biosciences Division, Mail Stop M888, Los Alamos, NM 87545
2 Life Sciences Division, Department of Cell and Molecular Biology, Lawrence Berkeley National Laboratory, Mail Stop 74-157, One Cyclotron Road, Berkeley, California 94720
* Corresponding author. E-mail address: rbcary{at}telomere.lanl.gov.
Several findings have revealed a likely role for DNA ligase IV, and interacting protein XRCC4, in the final steps of mammalian DNA double-strand break repair. Recent evidence suggests that the human DNA ligase IV protein plays a critical role in the maintenance of genomic stability. To identify protein-protein interactions that may shed further light on the molecular mechanisms of DSB repair and the biological roles of human DNA ligase IV, we have employed the yeast two-hybrid system in conjunction with traditional biochemical methods. These efforts have resulted in the identification of a physical association between the DNA ligase IV polypeptide and the human condensin subunit known as hCAP-E. The hCAP-E polypeptide, a member of the Structural Maintenance of Chromosomes (SMC) super-family of proteins, co-immunoprecipitates from cell extracts with DNA ligase IV. Immunofluorescence studies reveal co-localization of DNA ligase IV and hCAP-E in the interphase nucleus, while mitotic cells display co-localization of both polypeptides on mitotic chromosomes. Strikingly, the XRCC4 protein is excluded from the area of mitotic chromosomes, suggesting the formation of specialized DNA ligase IV complexes subject to cell cycle regulation. We discuss our findings in light of known and hypothesized roles for ligase IV and the condensin complex.
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