Histone H2B Monoubiquitination Functions Cooperatively with FACT to Regulate Elongation by RNA Polymerase II

To link to full-text access for this article, visit this link: http://dx.doi.org/10.1016/j.cell.2006.04.029 Byline: Rushad Pavri (1), Bing Zhu (1), Guohong Li (1), Patrick Trojer (1), Subhrangsu Mandal (1), Ali Shilatifard (2), Danny Reinberg (1) Abstract: Over the past years, a large number of histone posttranslational modifications have been described, some of which function to attain a repressed chromatin structure, while others facilitate activation by allowing access of regulators to DNA. Histone H2B monoubiquitination is a mark associated with transcriptional activity. Using a highly reconstituted chromatin-transcription system incorporating the inducible RAR[beta]2 promoter, we find that the establishment of H2B monoubiquitination by RNF20/40 and UbcH6 is dependent on the transcription elongation regulator complex PAF, the histone chaperone FACT, and transcription. H2B monoubiquitination facilitates FACT function, thereby stimulating transcript elongation and the generation of longer transcripts. These in vitro analyses and corroborating in vivo experiments demonstrate that elongation by RNA polymerase II through the nucleosomal barrier is minimally dependent upon (1) FACT and (2) the recruitment of PAF and the H2B monoubiquitination machinery. Author Affiliation: (1) Howard Hughes Medical Institute, Department of Biochemistry, Division of Nucleic Acids Enzymology, Robert Wood Johnson Medical School, University of Medicine and Dentistry of New Jersey, 683 Hoes Lane, Piscataway, NJ 08854, USA (2) Department of Biochemistry, Saint Louis University School of Medicine, 1402 South Grand Boulevard, Saint Louis, MI 63104, USA Article History: Received 9 February 2006; Revised 23 March 2006; Accepted 20 April 2006 Article Note: (miscellaneous) Published: May 18, 2006