Abstract：
: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.
journal_name
Phytochemistryjournal_title
Phytochemistryauthors
Mozgová I,Schrumpfová PP,Hofr C,Fajkus Jdoi
10.1016/j.phytochem.2008.04.001subject
Has Abstractpub_date
2008-06-01 00:00:00pages
1814-9issue
9eissn
0031-9422issn
1873-3700pii
S0031-9422(08)00179-9journal_volume
69pub_type
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