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.
- MeSH
- Arabidopsis genetika metabolismus MeSH
- DNA rostlinná metabolismus MeSH
- DNA vazebné proteiny genetika metabolismus MeSH
- elektroforéza v polyakrylamidovém gelu MeSH
- financování organizované MeSH
- histony metabolismus MeSH
- klonování DNA MeSH
- lidé MeSH
- onkogenní proteiny v-myb metabolismus MeSH
- proteiny huseníčku genetika metabolismus MeSH
- telomery metabolismus MeSH
- vazba proteinů MeSH
- Check Tag
- lidé MeSH
- Publikační typ
- abstrakt z konference MeSH
- MeSH
- financování organizované MeSH
- Publikační typ
- abstrakty MeSH
