NF-kappaB p52:RelB heterodimer recognizes two classes of kappaB sites with two distinct modes.
EMBO Rep
; 10(2): 152-9, 2009 Feb.
Article
em En
| MEDLINE
| ID: mdl-19098713
ABSTRACT
The X-ray structure of the nuclear factor-kappaB (NF-kappaB) p52RelBkappaB DNA complex reveals a new recognition feature not previously seen in other NF-kappaBkappaB DNA complexes. Arg 125 of RelB is in contact with an additional DNA base pair. Surprisingly, the p52RelB R125A mutant heterodimer shows defects both in DNA binding and in transcriptional activity only to a subclass of kappaB sites. We found that the Arg 125-sensitive kappaB sites contain more contiguous and centrally located AT base pairs than do the insensitive sites. A protein-induced kink observed in this complex, which used an AT-rich kappaB site, might allow the DNA contact by Arg 125; such a kink might not be possible in complexes with non-AT-rich kappaB sites. Furthermore, we show that the p52RelB heterodimer binds to a broader spectrum of kappaB sites when compared with the p50RelA heterodimer. We suggest that the p52RelB heterodimer is more adaptable to complement sequence and structural variations in kappaB sites when compared with other NF-kappaB dimers.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
DNA
/
Subunidade p52 de NF-kappa B
/
Fator de Transcrição RelB
Tipo de estudo:
Prognostic_studies
Limite:
Animals
/
Humans
Idioma:
En
Revista:
EMBO Rep
Assunto da revista:
BIOLOGIA MOLECULAR
Ano de publicação:
2009
Tipo de documento:
Article
País de afiliação:
Estados Unidos