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Our findings expand the clinical and molecular spectrum of homozygous PRMT7 mutations, associated to the SBIDDS syndrome, showing a possible correlation between the type of mutation and the severity of the phenotype.
These kinetic studies suggest a biochemical explanation for the interplay between PRMT5- and PRMT7-mediated methylation of the same substrate at different residues and also suggest a general model for regulation of PRMTs.
The authors showed that ASS1 mutations linked to type I citrullinemia disrupt the ASS1-PRMT7 interaction, which might explain the molecular pathogenesis of the disease.
Loss of PRMT7 causes decreases in arginine methylation throughout the proteome.Loss of the arginine methyltranserase PRMT7 causes syndromic intellectual disability with microcephaly and brachydactyly.
Upregulation of PRMT7 in breast cancer may have a significant role in promoting cell invasion through the regulation of MMP9.
results define PRMT7 as an inducer of breast cancer metastasis and present the opportunity for applying PRMT7-targeted therapeutics to treat highly invasive breast cancers
Data indicate that two acidic residues within the double E loop, Asp-147 and Glu-149, confer specificity to protein arginine methyltransferase 7 (PRMT7.
reducing expression of individual PRMT7 target DNA repair genes showed that only the catalytic subunit of DNA polymerase, POLD1, was able to resensitize PRMT7 knock-down cells to DNA-damaging agents.
Human protein arginine methyltransferase 7 (PRMT7) is a type III enzyme forming omega-NG-monomethylated arginine residues.
Here the authors report that H3R2 is also symmetrically dimethylated (H3R2me2s) by PRMT5 and PRMT7 and present in euchromatic regions.
both domains are required for functionality
PRMT7 (like PRMT5) is a Type II methyltransferase capable of producing symmetric dimethylarginine modifications in proteins.
that in human cells, PRMT5 and PRMT7 are required for Sm protein sDMA modification, and that Sm protein symmetric dimethylarginine modification is required for snRNP biogenesis in human cells.
Of the 28 proteins, only arginine methyltransferase 7 (PRMT7) changed substantially during mouse embryogenesis and promoted the conversion of mouse fibroblasts into iPSCs. Specifically, PRMT7 replaced SOX2 in a factor-substitution assay, yielding iPSCs
miR-24-2-5p is an anti-pluripotent miRNA involved in a novel epigenetic stemness-regulatory mechanism in which a double-negative feedback loop consisting of PRMT7 and miR-24-3p/miR24-2-5p interplays with Oct4, Nanog, Klf4 and c-Myc to control stemness.
Prmt7 is a key regulator for skeletal muscle oxidative metabolism. Prmt7 is expressed at the highest levels in skeletal muscle and decreased in skeletal muscles with age or obesity. Prmt7(-/-) muscles exhibit decreased oxidative metabolism with decreased expression of genes involved in muscle oxidative metabolism, including PGC-1alpha. Consistently, Prmt7(-/-) mice exhibited significantly reduced endurance exercise cap...
The findings define PRMT7 as a regulator of the DNMT3b/p21 axis required to maintain muscle stem cell regenerative capacity.
PRMT7 structure is composed of two catalytic modules in tandem forming a pseudo-dimer and contains only one AdoHcy molecule bound to the N-terminal module
PRMT7 could recruit H4R3me1 and symmetric H4R3me2 to the Bcl6 promoter. These results provide evidence for the important roles played by PRMT7 in germinal center formation.
Mammalian protein arginine methyltransferase 7 (PRMT7) specifically targets RXR sites in lysine- and arginine-rich regions.
CTCFL and PRMT7 may play a role in male germline imprinted gene methylation.
Data show that epiboly relies on the molecular networking of protein arginine methyltransferase 7 (Prmt7) by facilitating syntenin, which acts as a regulator for cytoskeleton.
Prmt7 regulates epiboly by facilitating 2-OST and modulating actin cytoskeleton
C. elegans PRMT-7 has a substrate specificity and a substrate preference different from those of mammalian PRMT7, and the available X-ray crystal structures of the PRMT7 orthologs show differences in active site architecture
Data indicate that only the N-terminal catalytic site of protein arginine methyltransferase 7 (PRMT7) is responsible for cofactor binding.
Arginine methylation is an apparently irreversible protein modification catalyzed by arginine methyltransferases, such as PMT7, using S-adenosylmethionine (AdoMet) as the methyl donor. Arginine methylation is implicated in signal transduction, RNA transport, and RNA splicing (Miranda et al., 2004
protein arginine methyltransferase 7
, [Myelin basic protein]-arginine N-methyltransferase PRMT7
, histone-arginine N-methyltransferase PRMT7
, myelin basic protein-arginine N-methyltransferase
, protein arginine N-methyltransferase 7
, arginine N-methyltransferase
, Histone-arginine N-methyltransferase PRMT7