Published online 18 February 2005
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The SAF-box domain of chromatin protein DEK
Department of Biology, University of Konstanz 78457 Konstanz, Germany 1 Department of Biochemistry, Molecular Biology and Biophysics, University of Minnesota Minneapolis, MN 55455, USA
*To whom correspondence should be addressed at Max Planck Institute for Immunology Stübeweg 51, D-79108 Freiburg, Germany. Tel: +49 761 5108377; Fax: +49 761 5108220; Email: Tanja.Waldmann{at}gmx.de
Received November 15, 2004. Revised January 31, 2005. Accepted January 31, 2005.
DEK is an abundant chromatin protein in metazoans reaching copy numbers of several millions/nucleus. Previous work has shown that human DEK, a protein of 375 amino acids, has two functional DNA-binding domains, of which one resides in a central part of the molecule and contains sequences corresponding to the scaffold attachment factor-box (SAF-box) domain as found in a growing number of nuclear proteins. Isolated SAF-box peptides (amino acids 137–187) bind weakly to DNA in solution, but when many SAF-box peptides are brought into close proximity on the surface of Sephadex beads, cooperative effects lead to a high affinity to DNA. Furthermore, a peptide (amino acids 87–187) that includes a sequence on the N-terminal side of the SAF-box binds efficiently to DNA. This peptide prefers four-way junction DNA over straight DNA and induces supercoils in relaxed circular DNA just like the full-length DEK. Interestingly, however, the 87–187 amino acid peptide introduces negative supercoils in contrast to the full-length DEK, which is known to introduce positive supercoils. We found that two adjacent regions (amino acids 68–87 and 187–250) are necessary for the formation of positive supercoils. Our data contribute to the ongoing characterization of the abundant and ubiquitous DEK chromatin protein.
The authors wish it to be known that, in their opinion, the first two authors should be regarded as joint First Authors
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