Examination of histone H2B ubiquitination in wild type and USP49 knockdown cells [ChIP-Seq]

ABSTRACT: Posttranslational histone modifications play important roles in regulating chromatin structure and function. Histone H2B ubiquitination and deubiquitination have been implicated in transcriptional regulation, but the function of H2B deubiquitination is not well defined, particularly in higher eukaryotes. Here we report the purification of USP49 as a histone H2B specific deubiquitinase and demonstrate that H2B deubiquitination by USP49 is required for efficient co-transcriptional splicing of a large set of exons. USP49 forms a complex with RVB1 and SUG1, and specifically deubiquitinates histone H2B in vitro and in vivo. USP49 knockdown results in small changes in gene expression, but affects the abundance of over 9,000 isoforms. Exons down-regulated in USP49 knockdown cells show both eleva

ORGANISM(S): Homo sapiens

SUBMITTER: Hengbin Wang 

PROVIDER: E-GEOD-38099 | biostudies-arrayexpress |

REPOSITORIES: biostudies-arrayexpress