Functional characterization of domains in AtTRB1, a putative telomere-binding protein in Arabidopsis thaliana.
Phytochemistry
; 69(9): 1814-9, 2008 Jun.
Article
en En
| MEDLINE
| ID: mdl-18479720
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.
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Telómero
/
Arabidopsis
/
Proteínas de Arabidopsis
/
Proteínas de Unión al ADN
Límite:
Humans
Idioma:
En
Revista:
Phytochemistry
Año:
2008
Tipo del documento:
Article
País de afiliación:
República Checa