Journal
PHYTOCHEMISTRY
Volume 69, Issue 9, Pages 1814-1819Publisher
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.phytochem.2008.04.001
Keywords
plant; Arabidopsis thaliana; telomere; Single-Myb-Histone protein; AtTRB1; DNA-protein interaction; EMSA; PFO-ELFO
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Telomeres are nucleoprotein structures ensuring the stability of eukaryotic chromosome ends. Two protein families, TRFL (TFL-Like) and SMH (Single-Myb-Histone), containing a specific telobox motif in their Myb domain, have been identified as potential candidates involved in a functional nucleoprotein structure analogous to human shelterin at plant telomeres. We analyze the DNA-protein interaction of the full-length and truncated variants of AtTRB1, a SMH-family member with a typical structure: N-terminal Myb domain, central H1/5 domain and C-terminal coiled-coil. We show that preferential interaction of AtTRB1 with double-stranded telomeric DNA is mediated by the Myb domain, while the H1/5 domain is involved in non-specific DNA-protein interaction and in the multimerization of AtTRB1. (C) 2008 Elsevier Ltd. All rights reserved.
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