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Nucleic Acids Research Advance Access originally published online on October 4, 2006
Nucleic Acids Research 2006 34(19):5541-5551; doi:10.1093/nar/gkl685
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Nucleic Acids Research, 2006, Vol. 34, No. 19 5541-5551
© 2006 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

Nucleic Acid Enzymes

Purification of the yeast Slx5–Slx8 protein complex and characterization of its DNA-binding activity

Litao Yang, Janet R. Mullen and Steven J. Brill*

Department of Molecular Biology and Biochemistry, Rutgers University Piscataway, NJ 08854, USA

*To whom correspondence should be addressed at Department of Molecular Biology and Biochemistry, 679 Hoes Lane, CABM, Rutgers University, Piscataway, NJ 08854, USA. Tel: +1 732 235 4197; Fax: +1 732 235 4880; Email: brill{at}mbcl.rutgers.edu

Received April 3, 2006. Revised August 14, 2006. Accepted September 7, 2006.

SLX5 and SLX8 encode RING-finger proteins that were previously identified based on their requirement for viability in yeast cells lacking Sgs1 DNA helicase. Slx5 and Slx8 proteins are known to be required for genome stability and to physically interact in yeast extracts; however, their biochemical functions are unknown. To address this question we purified and characterized recombinant Slx5 and Slx8 proteins. Here we show that Slx5 and Slx8 form a heterodimeric complex with double-stranded DNA (dsDNA)-binding activity. Individually, only the Slx8 subunit displays this activity. Structure–function studies indicate that the DNA-binding activity requires only the N-terminal 160 amino acids of Slx8, but not its C-terminal RING-finger domain. Alleles of SLX8 that express the RING-finger domain alone show almost complete complementation in yeast indicating that this DNA-binding domain is not essential for this in vivo function. Consistent with these findings we show that Slx5 immunolocalizes to the nucleus and that a portion of the Slx8 protein co-fractionates with chromatin. These results suggest that Slx5–Slx8 may act directly on DNA to promote genome stability.


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