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PMID: 16713563 Published · ppublish English Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't

Histone H2B monoubiquitination functions cooperatively with FACT to regulate elongation by RNA polymerase II.

Cell ·Vol. 125 ·No. 4 ·2006-05-19 ·Pages 703-17

Pavri R, Zhu B, Li G, Trojer P, Mandal S, Shilatifard A, Reinberg D

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 RARbeta2 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.

MeSH Terms
Animals Chromatin/metabolism DNA-Binding Proteins/metabolism High Mobility Group Proteins/metabolism Histones/metabolism Humans Macromolecular Substances Nucleosomes/metabolism Peptide Chain Elongation, Translational Promoter Regions, Genetic RNA Polymerase II/metabolism Receptors, Retinoic Acid/genetics,metabolism Transcription, Genetic Transcriptional Activation Transcriptional Elongation Factors/metabolism Ubiquitin/metabolism
Chemicals
Chromatin DNA-Binding Proteins High Mobility Group Proteins Histones Macromolecular Substances Nucleosomes Receptors, Retinoic Acid SSRP1 protein, human Transcriptional Elongation Factors Ubiquitin retinoic acid receptor beta RNA Polymerase II
Authors & Affiliations
7 authors, click to expand affiliations / ORCID
Pavri Rushad
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.
Zhu Bing
Li Guohong
Trojer Patrick
Mandal Subhrangsu
Shilatifard Ali
Reinberg Danny
Article Info
Journal
Cell
Abbr.
Cell
ISSN
0092-8674
Published
2006-05-19
Pages
703-17
Language
English
Region
United States
NLM ID
0413066
Subset
IM
Grants
NIGMS NIH HHS · GM37120 · United States
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