Physical association between the histone acetyl transferase CBP and a histone methyl transferase
AUTOR(ES)
Vandel, Laurence
FONTE
Oxford University Press
RESUMO
CBP (CREB-binding protein) is involved in transcriptional activation by a great variety of sequence-specific transcription factors. CBP has been shown to activate transcription through its histone acetyl transferase activity. Acetylation is a common post-translational modification of nucleosomal histone N-terminal tails, which generally correlates with transcriptional activation. Histone N-terminal tails are also modified by methylation but its functional consequences are largely unknown. Here we found that immunoprecipitation of CBP, or of the highly related p300, led to the co-immunoprecipitation of a robust histone methyl transferase (HMT) activity, indicating that CBP physically interacts with an HMT in living cells. The CBP-associated HMT is specific for lysines 4 and 9 of histone H3, which are known to be methylated in living cells. These results suggest that histone methylation could be involved in transcriptional activation. Furthermore, they raise the question of the link between histone methylation and acetylation.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=1083799Documentos Relacionados
- Functional and physical interaction between the histone methyl transferase Suv39H1 and histone deacetylases
- A rapid and sensitive assay for histone acetyl-transferase activity.
- Rhizobial NodL O-Acetyl Transferase and NodS N-Methyl Transferase Functionally Interfere in Production of Modified Nod Factors
- Physical and functional association of glycolipid N-acetyl-galactosaminyl and galactosyl transferases in the Golgi apparatus
- Association between daily physical activity and neighborhood environments