δ-N-Methylarginine Is a Novel Posttranslational Modification of Arginine Residues in Yeast Proteins
TLDR
It is suggested that the identity of the original unknown methylated residue is δ-N-monomethylarginine, a novel type of protein modification reaction in eukaryotes.About:
This article is published in Journal of Biological Chemistry.The article was published on 1998-11-06 and is currently open access. It has received 64 citations till now. The article focuses on the topics: Ion chromatography & Arginine.read more
Citations
More filters
Journal ArticleDOI
The key to development: interpreting the histone code?
TL;DR: Evidence is provided that the enzymes responsible for the modifications of histones function in a coordinated pattern to control gene expression in the short term and, through the transferral of these modifications by inheritance to their progeny, in the long term.
Journal ArticleDOI
Detection technologies in proteome analysis
TL;DR: New multiplexing capabilities should greatly enhance the applicability of the two-dimensional gel electrophoresis technique with respect to addressing fundamental questions related to proteome-wide changes in protein expression and post-translational modification.
Journal ArticleDOI
PRMT1 Is the Predominant Type I Protein Arginine Methyltransferase in Mammalian Cells
Jie Tang,Adam Frankel,Robert J. Cook,Sangduk Kim,Woon Ki Paik,Kenneth R. Williams,Steven Clarke,Harvey R. Herschman +7 more
TL;DR: It is concluded that PRMT1 contributes the major type I protein arginine methyltransferase enzyme activity present in mammalian cells and tissues.
Journal ArticleDOI
PRMT5 (Janus kinase-binding protein 1) catalyzes the formation of symmetric dimethylarginine residues in proteins.
Tina L. Branscombe,Adam Frankel,Jin Hyung Lee,Jeffry R. Cook,Zhi-Hong Yang,Sidney Pestka,Steven Clarke +6 more
TL;DR: PRMT5 is the first example of a catalytic chain for a type II protein arginine N-methyltransferase that can result in the formation of symmetric dimethylarginine residues as observed previously in myelin basic protein, Sm small nuclear ribonucleoproteins, and other polypeptides.
Journal ArticleDOI
Protein arginine methyltransferases: evolution and assessment of their pharmacological and therapeutic potential.
TL;DR: Because of the intricate involvement of several PRMT in cellular physiology, their inhibition may be fraught with unwanted side effects, Nevertheless, development of pharmaceutical agents to control PRMT functions could lead to significant new targets.
References
More filters
Book ChapterDOI
RNA and Protein Interactions Modulated by Protein Arginine Methylation
Jonathan D. Gary,Steven Clarke +1 more
TL;DR: From the analysis of the sequences surrounding known arginine methylation sites, consensus methyl-accepting sequences are determined that may be useful in identifying novel substrates for these enzymes and may shed further light on their physiological role.
Journal ArticleDOI
Widespread occurrence of three sequence motifs in diverse S-adenosylmethionine-dependent methyltransferases suggests a common structure for these enzymes.
Ron M. Kagan,Steven Clarke +1 more
TL;DR: Three regions of sequence similarity have been reported in several protein and small-molecule S-adenosylmethionine-dependent methyltransferases and it is suggested that these conserved regions contribute to the binding of the substrate S-ADenosyl methionines and/or the product S- adenosylhomocysteine.
Journal ArticleDOI
In Vivo and In Vitro Arginine Methylation of RNA-Binding Proteins
Qing Liu,Gideon Dreyfuss +1 more
TL;DR: This work partially purified and characterized a protein-arginine N-methyltransferase specific for hnRNPs from HeLa cells and demonstrated that most of the pre-mRNA-binding proteins receive this modification.
Journal ArticleDOI
PRMT 3, a type I protein arginine N-methyltransferase that differs from PRMT1 in its oligomerization, subcellular localization, substrate specificity, and regulation
TL;DR: A recombinant glutathione S-transferase (GST) fusion product of this new rat protein, named PRMT3, asymmetrically dimethylates arginine residues present both in the designed substrate GST-GAR and in substrate proteins present in hypomethylated extracts of a yeast rmt1 mutant that lacks type I N-methyltransferase activity as discussed by the authors.
Related Papers (5)
RNA and Protein Interactions Modulated by Protein Arginine Methylation
Jonathan D. Gary,Steven Clarke +1 more