Symmetrical dimethylation of arginine residues in spliceosomal Sm protein B/B′ and the Sm-like protein LSm4, and their interaction with the SMN protein

Arginine residues in RG-rich proteins are frequently dimethylated posttranslationally by protein arginine methyltransferases (PRMTs). The most common methylation pattern is asymmetrical dimethylation, a modification important for protein shuttling and signal transduction. Symmetrically dimethylated...

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Veröffentlicht in:	RNA (Cambridge) 2001-11, Vol.7 (11), p.1531-1542, Article S135583820101442X
Hauptverfasser:	BRAHMS, HERO, MEHEUS, LYDIE, DE BRABANDERE, VERONIQUE, FISCHER, UTZ, LÜHRMANN, REINHARD
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Arginine - metabolism Autoantigens - metabolism B/B protein Cyclic AMP Response Element-Binding Protein Cytoplasm - metabolism HeLa Cells Humans LSm4 protein Methylation Molecular Sequence Data Nerve Tissue Proteins - metabolism protein arginine methyltransferases Protein Processing, Post-Translational Ribonucleoproteins, Small Nuclear - metabolism RNA-Binding Proteins S-adenosylhomocysteine SMN Complex Proteins snRNP Core Proteins spinal muscular atrophy Spliceosomes - metabolism UsnRNP protein
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