Histone deimination antagonizes arginine methylation Journal Article

Authors: Cuthbert, G. L.; Daujat, S.; Snowden, A. W.; Erdjument-Bromage, H.; Hagiwara, T.; Yamada, M.; Schneider, R.; Gregory, P. D.; Tempst, P.; Bannister, A. J.; Kouzarides, T.
Article Title: Histone deimination antagonizes arginine methylation
Abstract: Methylation of arginine residues within histone H3 has been linked to active transcription. This modification appears on the estrogen-regulated pS2 promoter when the CARM1 methyltransferase is recruited during transcriptional activation. Here we describe a process, deimination, that converts histone arginine to citrulline and antagonizes arginine methylation. We show that peptidyl arginine deiminase 4 (PADI4) specifically deiminates, arginine residues R2, R8, R17, and R26 in the H3 tail. Deimination by PADI4 prevents arginine methylation by CARM1. Dimethylation of arginines prevents deimination by PADI4 although monomethylation still allows deimination to take place. In vivo targeting experiments on an endogenous promoter demonstrate that PADI4 can repress hormone receptor-mediated gene induction. Consistent with a repressive role for PADI4, this enzyme is recruited to the pS2 promoter following hormone induction when the gene is transcriptionally downregulated. The recruitment of PADI4 coincides with deimination of the histone H3 N-terminal tail. These results define deimination as a novel mechanism for antagonizing the transcriptional induction mediated by arginine methylation.
Keywords: controlled study; methylation; promoter region; proteins; protein targeting; genetic transcription; cell line, tumor; molecular mechanics; gene expression regulation; amino terminal sequence; protein synthesis; histone; gene repression; tumor suppressor proteins; protein structure, tertiary; down regulation; gene induction; molecular interaction; molecular biology; hormonal regulation; histones; protein derivative; arginine; gene expression regulation, enzymologic; hydrolases; promoter regions (genetics); trans-activation (genetics); protein-arginine n-methyltransferase; arginine derivative; citrulline; humans; human; priority journal; article; imine; imines
Journal Title: Cell
Volume: 118
Issue: 5
ISSN: 0092-8674
Publisher: Cell Press  
Date Published: 2004-09-03
Start Page: 545
End Page: 553
Language: English
DOI: 10.1016/j.cell.2004.08.020
PROVIDER: scopus
PUBMED: 15339660
Notes: Cell -- Cited By (since 1996):396 -- Export Date: 16 June 2014 -- CODEN: CELLB -- Source: Scopus
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MSK Authors
  1. Paul J Tempst
    323 Tempst