Highly acidic C-terminal domain of pp32 is required for the interaction with histone chaperone, TAF-Ibeta.
Biol Pharm Bull
; 29(12): 2395-8, 2006 Dec.
Article
em En
| MEDLINE
| ID: mdl-17142970
ABSTRACT
We have previously reported that INHAT (inhibitor of acetyltransferases) complex subunits, TAF (template activating factor)-Ialpha, TAF-Ibeta and pp32 can inhibit histone acetylation and HAT (histone acetyltransferase)-dependent transcription by binding to histones. Evidences are accumulating that INHAT complex subunits have important regulatory roles in various cellular activities such as replication, transcription, and apoptosis etc. However, how these subunits interact each other remains largely unknown. Using immunoprecipitation (IP) and protein-protein interaction assays with TAF-Ibeta and pp32 deletion mutant proteins, we identify INHAT complex subunits, TAF-Ibeta and pp32 interaction requires highly acidic C-terminal domain of pp32. We also show that the interaction between the INHAT complex subunits is stronger in the presence of histones. In this study, we report that the synergistic inhibition of HAT-mediated transcription by TAF-Ibeta and pp32 is dependent on the highly acidic C-terminal domain of pp32.
Buscar no Google
Base de dados:
MEDLINE
Assunto principal:
Fatores de Transcrição
/
Ácidos
/
Proteínas Nucleares
/
Proteínas Cromossômicas não Histona
Idioma:
En
Ano de publicação:
2006
Tipo de documento:
Article