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.Detection of the interaction between histone H3 lysine 9 acetylation and the RNA-binding protein RBM10 using an in vitro system.
We have previously demonstrated that histone acetylation at lysine 9 of histone H3 is associated with transcriptional activation. The RNA-binding protein RBM10 is a known component of transcriptional activation complexes and contains a tripartite domain encompassing three RNA-recognition motifs. In the present study, we found that the histone acetyltransferase CREB-binding protein (CBP) interacted with RBM10, and that the association was mediated by an RNA-binding domain of RBM10 and one of the CBP-associated factor (CAF) domains of CBP. Furthermore, the mutations of the catalytic lysine residues of CBP or RBM10 disrupted the interaction between these two proteins. These results strongly suggest that CBP might interact with RBM10 through its histone acetyltransferase activity and the RNA-binding domain of RBM10.segunda-feira, fevereiro 14, 2006

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