High-throughput sequence data of ChIP performed with anti-SMARCAD1 (ASNA) or anti-CBP actibodies.

Histone acetylation and nucleosome remodeling play a pivotal role in transcriptional regulation. While histone acetylase and ATP-dependent chromatin remodeling activities have been well characterized, how the two activities are coordinated remains to be uncovered. We discovered ATP-dependent histone H2A acetylation activity in Drosophila nuclear extracts. This activity was column-purified and demonstrated to be composed of CBP and SMARCAD1, which belongs to the Etl1 subfamily of the Snf2 family of helicase-related proteins. SMARCAD1 enhanced acetylation of H2A K5 and K8 by CBP in nucleosomes in an ATP-dependent fashion. Expression array analysis of S2 cells having ectopically expressed SMARCAD1 revealed up-regulated genes. Using native genome templates of these up-regulated genes, we found that SMARCAD1 activates their transcription in vitro. Knockdown analysis of SMARCAD1 and CBP indicated overlapping gene control, and ChIP-seq analysis of these commonly controlled genes showed that CBP is recruited to the promoter prior to SMARCAD1. Moreover, Drosophila genetic experiments demonstrated interaction between SMARCAD1/Etl1 and CBP/nej during development. The interplay between the remodeling activity of SMARCAD1 and histone acetylation by CBP sheds light on chromatin and the genome-integrity network. Examination of 2 different protein in 1 cell type.