Arginine Methylation

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Histone Deimination Antagonizes Arginine Methylation

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 deim...

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Arginine methylation at a glance.

Arginine methylation is a prevalent post-translational modification found on both nuclear and cytoplasmic proteins. The methylation of arginine residues is catalyzed by the protein arginine Nmethyltransferase (PRMT) family of enzymes. Proteins that are arginine methylated are involved in a number of different cellular processes, including transcriptional regulation, RNA metabolism and DNA damag...

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Analysis of protein arginine methylation and protein arginine-methyltransferase activity.

Posttranslational modification of proteins allows cells to adapt and react quickly to their environment beyond the boundaries set forth by genetic code. Arginine methylation, a protein modification discovered almost 30 years ago, has recently experienced a renewed interest as several new arginine methyltransferases have been identified and numerous proteins were found to be regulated by methyla...

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Arginine Methylation of STAT1 A Reassessment

Matters Arising sequent fluorography of two independent experiments revealed methylation of several proteins but not of STAT1

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Protein arginine methylation during lytic adenovirus infection.

Arginine methylation of proteins affects major processes in the cell, including transcriptional regulation, mRNA metabolism, signal transduction and protein sorting. Arginine methylation of Ad (adenovirus) E1B 55-kDa-associated protein E1B-AP5 was recently described by us [Kzhyshkowska, Schutt, Liss, Kremmer, Stauber, Wolf and Dobner (2001) Biochem. J. 358, 305-314]. In this first example of pr...

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ژورنال

عنوان ژورنال: Molecular Cell

سال: 2005

ISSN: 1097-2765

DOI: 10.1016/j.molcel.2005.04.003