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Abstract

Histone deimination antagonizes arginine methylation.
Cuthbert GL, Daujat S, Snowden AW, Erdjument-Bromage H, Hagiwara T,
Yamada M, Schneider R, Gregory PD, Tempst P, Bannister AJ, Kouzarides T.
Gurdon Institute and Department of Pathology, University of Cambridge,
Tennis Court Road, Cambridge CB2 1QR, United Kingdom.
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.