PRMT1 Is the Predominant Type I Protein Arginine Methyltransferase in Mammalian Cells*

@article{Tang2000PRMT1IT,
  title={PRMT1 Is the Predominant Type I Protein Arginine Methyltransferase in Mammalian Cells*},
  author={J. Tang and A. Frankel and R. Cook and S. Kim and W. Paik and K. Williams and S. Clarke and H. Herschman},
  journal={The Journal of Biological Chemistry},
  year={2000},
  volume={275},
  pages={7723 - 7730}
}
Type I protein arginine methyltransferases catalyze the formation of asymmetric ω-N G,N G-dimethylarginine residues by transferring methyl groups fromS-adenosyl-l-methionine to guanidino groups of arginine residues in a variety of eucaryotic proteins. The predominant type I enzyme activity is found in mammalian cells as a high molecular weight complex (300–400 kDa). In a previous study, this protein arginine methyltransferase activity was identified as an additional activity of 10… Expand
The Novel Human Protein Arginine N-Methyltransferase PRMT6 Is a Nuclear Enzyme Displaying Unique Substrate Specificity*
TLDR
This novel human PRMT, which resides solely in the nucleus when fused to the green fluorescent protein, joins a family of enzymes with diverse functions within cells and displays automethylation activity; it is the first PRMT to do so. Expand
PRMT3 Is a Distinct Member of the Protein Arginine N-Methyltransferase Family
TLDR
The treatment of RAT1 cell extracts with N-ethylmaleimide leads to a loss of the major PRMT1-associated activity that was immune to inhibition under the same conditions as a GST fusion protein, suggesting that native forms of PRMTs can have different properties than their GST-catalytic chain fusion protein counterparts, which may lack associated noncatalysttic subunits. Expand
Regulation of Protein Arginine Methyltransferase 8 (PRMT8) Activity by Its N-terminal Domain*
TLDR
It is shown here that both His-tagged and GST fusion species lacking the initial 60 amino acid residues of PRMT8 have enhanced enzymatic activity, suggesting that the N-terminal domain may regulate PRMT6 activity and may function as an autoregulator that is displaced by interaction with one or more physiological inducers. Expand
Characterization of protein arginine methyltransferases in porcine brain.
TLDR
The results suggest that part of the type I arginine methyltransferases in brains, mainly PRMT1, are sequestered in an inactive form as they associated with membranes or large subcellular complexes. Expand
Protein arginine methyltransferase I: Substrate specificity and role in hnRNP assembly
TLDR
Methylation of the most abundant Prmt1 substrates appeared to be extensive and constitutive throughout the cell cycle, suggesting the modification does not modulate protein function under normal growth conditions. Expand
Multimerization of expressed protein-arginine methyltransferases during the growth and differentiation of rat liver.
TLDR
It is observed that PRMTs are catalytically active only in the form of multimers, but not as a dimer or tetramer of the expressed subunit, and thus, some uncharacterized additional factor(s) may multimerizePRMTs to express catalytic activities in vivo. Expand
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TLDR
The design, synthesis, and characterization of fluorescein-conjugated C21 (F-C21) and biotin-con conjugated C 21 (B-C 21) are reported as PRMT1-specific ABPs, providing the first evidence thatPRMT1 activity is negatively regulated in a spatial and temporal fashion. Expand
Dynamics of Human Protein Arginine Methyltransferase 1(PRMT1) in Vivo*
TLDR
It is shown that only a fraction of PRMT1 is located in the nucleus, but the protein is predominantly cytoplasmic, suggesting a mechanism where PR MT1 is trapped by unmethylated substrates such as core histones and heterogeneous nuclear ribonucleoprotein proteins until it has executed the methylation reaction. Expand
PRMT5, Which Forms Distinct Homo-oligomers, Is a Member of the Protein-arginine Methyltransferase Family*
TLDR
Results indicate that both covalent linkage by a disulfide bond and noncovalent association are involved in the formation of PRMT5 homo-oligomers, which appears to have lower specific enzyme activity than PRMT1. Expand
PRMT8, a New Membrane-bound Tissue-specific Member of the Protein Arginine Methyltransferase Family*
TLDR
It is shown here that PRMT8 is indeed modified by the attachment of a myristate to the glycine residue after the initiator methionine, and it is thus an active arginine methyltransferase that is membrane-associated and tissue-specific, two firsts for this family of enzymes. Expand
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References

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PRMT 3, a Type I Protein Arginine N-Methyltransferase That Differs from PRMT1 in Its Oligomerization, Subcellular Localization, Substrate Specificity, and Regulation*
Methylation is one of the many post-translational modifications that modulate protein function. Although asymmetricN G,N G-dimethylation of arginine residues in glycine-arginine-rich domains ofExpand
RNase treatment of yeast and mammalian cell extracts affects in vitro substrate methylation by type I protein arginine N-methyltransferases.
TLDR
The results suggest that the methylation and RNA-binding of GAR domain-containing proteins in vivo may regulate protein-nucleic acid or protein-protein interactions. Expand
The Predominant Protein-arginine Methyltransferase from Saccharomyces cerevisiae(*)
TLDR
RMT1 appears to be a yeast homolog of a recently characterized mammalian protein-arginine methyltransferase whose activity may be modulated by mitotic stimulation of cells. Expand
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. Expand
Purification and characterization of S-adenosylmethionine-protein-arginine N-methyltransferase from rat liver.
A protein methylase I (S-adenosylmethionine-protein-arginine N-methyltransferase; EC 2.1.1.23), with a high specificity for recombinant heterogeneous nuclear ribonucleoprotein particle (hnRNP)Expand
S-adenosylmethionine: protein-arginine methyltransferase. Purification and mechanism of the enzyme.
TLDR
The results suggest that the mechanism of the protein methylase I reaction is a Sequential Ordered Bi Bi mechanism with S-adenosyl-L-methionine as the first substrate, histone H4 as the second substrate, methylated hist one H4As the first product, and S- adenosyl -L-homocysteine asThe second product released. Expand
Identification of Protein-ArginineN-Methyltransferase as 10-Formyltetrahydrofolate Dehydrogenase*
TLDR
Data base searching of both the mass spectrometric and Edman sequencing data from several peptides identified the protein methylase as 10-formyltetrahydrofolate dehydrogenase and this identification was confirmed by comparative HPLC tryptic peptide mapping and affinity chromatography of the methylase on the 5-forms-of-forms affinity gel used to purify the dehydrogenases. Expand
In vivo and in vitro arginine methylation of RNA-binding proteins.
TLDR
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. Expand
Purification and molecular identification of two protein methylases I from calf brain. Myelin basic protein- and histone-specific enzyme.
TLDR
Two different molecular species of protein methylases I, one specific for myelin basic protein (MBP) and the other for histone, have been purified from calf brain to near homogeneity, as discerned by nondenaturing polyacrylamide gel electrophoresis. Expand
The Mammalian Immediate-early TIS21 Protein and the Leukemia-associated BTG1 Protein Interact with a Protein-arginine N-Methyltransferase*
TLDR
Modulation of PRMT1 activity by transiently expressed regulatory subunits may be an additional mode of signal transduction following ligand stimulation followingligand stimulation. Expand
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