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The polyadendylation factor CPSF-73 is involved in histone-pre-mRNA processing

Article Abstract:

UV crosslinking studies were carried out using both the complete RNA substrate and the downstream cleavage product, each containing a single radioactive phosphate and a phosphorothiolate modification at the cleavage site. It is suggested that cleavage/polyadenylation specificity factor-73 (CPSF-73) is both the endonuclease and 5',3' exonuclease in histone-pre-mRNA processing and reveal an evolutionary link between 3' end formation of histone mRNAs and polyadenylated mRNAs.

Author: Marzluff, William F., Dominiski, Zbigniew, Xiao-cui Yang
Publisher: Elsevier B.V.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 2005
RNA processing, Ribonucleoproteins

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Reversal of histone lysine trimethylation by the JMJD2 family of histone demethylases

Article Abstract:

The JmjC domain-containing protein JMJD2A reversed trimethylated H3-K9/K36 trimethylation levels in cultured cells. The findings that this family of demethylases generates different methylated states at the same lysine residue provides a mechanism for fine-tuning histone methylation.

Author: Whetstine, Johnathan R., Yang Shi, Zhongzhou Chen, Nottke, Amanda; Spooner, Eric, Fei Lan; En Li, Huarte, Malte; Gongyi Zhang, Smolikov, Sarit, Colalacovo, Monica
Publisher: Elsevier B.V.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 2006
Lysine

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Histone deimination antagonizes arginine methylation

Article Abstract:

A process called deimination that converts histone arginine to citrulline and antagonizes arginine methylation is discussed. The results show that deimination is a unique mechanism for antagonizing the transcriptional induction through arginine methylation.

Author: Cuthbert, Graeme L., Daujat, Sylvain
Publisher: Elsevier B.V.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 2004
Methods, Arginine, Chemical properties

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Subjects list: Research, Histones, Methylation
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