Millipore Sigma Vibrant Logo
 

1.07414


21 Results Advanced Search  
Showing
Products (2)
Documents (19)
Site Content (0)

Narrow Your Results Use the filters below to refine your search

Document Type

  • (11)
  • (5)
  • (3)
Can't Find What You're Looking For?
Contact Customer Service

 

  • Characterization of the PRMT gene family in rice reveals conservation of arginine methylation. 21853042

    Post-translational methylation of arginine residues profoundly affects the structure and functions of protein and, hence, implicated in a myriad of essential cellular processes such as signal transduction, mRNA splicing and transcriptional regulation. Protein arginine methyltransferases (PRMTs), the enzymes catalyzing arginine methylation have been extensively studied in animals, yeast and, to some extent, in model plant Arabidopsis thaliana. Eight genes coding for the PRMTs were identified in Oryza sativa, previously. Here, we report that these genes show distinct expression patterns in various parts of the plant. In vivo targeting experiment demonstrated that GFP-tagged OsPRMT1, OsPRMT5 and OsPRMT10 were localized to both the cytoplasm and nucleus, whereas OsPRMT6a and OsPRMT6b were predominantly localized to the nucleus. OsPRMT1, OsPRMT4, OsPRMT5, OsPRMT6a, OsPRMT6b and OsPRMT10 exhibited in vitro arginine methyltransferase activity against myelin basic protein, glycine-arginine-rich domain of fibrillarin and calf thymus core histones. Furthermore, they depicted specificities for the arginine residues in histones H3 and H4 and were classified into type I and Type II PRMTs, based on the formation of type of dimethylarginine in the substrate proteins. The two homologs of OsPRMT6 showed direct interaction in vitro and further titrating different amounts of these proteins in the methyltransferase assay revealed that OsPRMT6a inhibits the methyltransferase activity of OsPRMT6b, probably, by the formation of heterodimer. The identification and characterization of PRMTs in rice suggests the conservation of arginine methylation in monocots and hold promise for gaining further insight into regulation of plant development.
    Document Type:
    Reference
    Product Catalog Number:
    Multiple
    Product Catalog Name:
    Multiple

  • COA 107414

    Document Type:
    Certificate of Analysis
    Product Catalog Number:
    107414

  • PRMT1 interacts with AML1-ETO to promote its transcriptional activation and progenitor cell proliferative potential. 22498736

    Fusion protein AML1-ETO, resulting from t(8;21) translocation, is highly related to leukemia development. It has been reported that full-length AML1-ETO blocks AML1 function and requires additional mutagenic events to promote leukemia. We have previously shown that the expression of AE9a, a splice isoform of AML1-ETO, can rapidly cause leukemia in mice. To understand how AML1-ETO is involved in leukemia development, we took advantage of our AE9a leukemia model and sought to identify its interacting proteins from primary leukemic cells. Here, we report the discovery of a novel AE9a binding partner PRMT1 (protein arginine methyltransferase 1). PRMT1 not only interacts with but also weakly methylates arginine 142 of AE9a. Knockdown of PRMT1 affects expression of a specific group of AE9a-activated genes. We also show that AE9a recruits PRMT1 to promoters of AE9a-activated genes, resulting in enrichment of H4 arginine 3 methylation, H3 Lys9/14 acetylation, and transcription activation. More importantly, knockdown of PRMT1 suppresses the self-renewal capability of AE9a, suggesting a potential role of PRMT1 in regulating leukemia development.
    Document Type:
    Reference
    Product Catalog Number:
    Multiple
    Product Catalog Name:
    Multiple

  • Carbon monoxide stimulates global protein methylation via its inhibitory action on cystathionine β-synthase. 21297920

    Although carbon monoxide derived from heme oxygenase has been reported to exert diverse biological actions in mammals, macromolecules responsible for its direct reception and functional outcomes of the gas binding remain largely unknown. Based on our previous results in vivo suggesting carbon monoxide serves as an inhibitor of cystathionine β-synthase that rate-limits transsulfuration pathway for generation of hydrogen sulfide, we have herein hypothesized that the gas might serve as a regulator of protein methylation through accelerating turnover of remethylation cycle residing at the upstream of the enzyme. Metabolomic analysis in human monoblastic leukemia U937 cells in culture revealed that application of carbon monoxide-releasing molecules caused increases in methionine and S-adenosylmethionine and a decrease in cystathionine in the cells, suggesting the cystathionine β-synthase inhibition by carbon monoxide. Under these circumstances, the cells exhibited global protein arginine methylation: this event was also reproduced by the cell treatment with hemin, a heme oxygenase-1 inducer. The protein arginine methylation elicited by carbon monoxide was attenuated by knocking down cystathionine β-synthase with its small interfering RNA or by blocking S-adenosylhomocysteine hydrolase with adenosine dialdehyde, suggesting remethylation cycling is necessary to trigger the methylation processing. Furthermore, proteins undergoing the carbon monoxide-induced arginine methylation involved histone H3 proteins, suggesting chromatin modification by the gas. Collectively with our studies in vivo showing its inhibitory action on endogenous hydrogen sulfide production, the current results suggest that not only inhibition of transsulfuration pathway for H(2)S generation but also activation of protein methylation accounts for notable biological actions of carbon monoxide via the cystathionine β-synthase inhibition.
    Document Type:
    Reference
    Product Catalog Number:
    Multiple
    Product Catalog Name:
    Multiple

  • Arginine methylation of ribosomal protein S3 affects ribosome assembly. 19460357

    The human ribosomal protein S3 (rpS3), a component of the 40S small subunit in the ribosome, is a known multi-functional protein with roles in DNA repair and apoptosis. We recently found that the arginine residue(s) of rpS3 are methylated by protein arginine methyltransferase 1 (PRMT1). In this paper, we confirmed the arginine methylation of rpS3 protein both in vitro and in vivo. The sites of arginine methylation are located at amino acids 64, 65 and 67. However, mutant rpS3 (3RA), which cannot be methylated at these sites, cannot be transported into the nucleolus and subsequently incorporated into the ribosome. Our results clearly show that arginine methylation of rpS3 plays a critical role in its import into the nucleolus, as well as in small subunit assembly of the ribosome.
    Document Type:
    Reference
    Product Catalog Number:
    07-414
    Product Catalog Name:
    Anti-dimethyl-Arginine Antibody, asymmetric (ASYM24)

  • hCAF1, a new regulator of PRMT1-dependent arginine methylation. 17264152

    Protein arginine methylation is an emergent post-translational modification involved in a growing number of cellular processes, including transcriptional regulation, cell signaling, RNA processing and DNA repair. Although protein arginine methyltransferase 1 (PRMT1) is the major arginine methyltransferase in mammals, little is known about the regulation of its activity, except for the regulation induced by interaction with the antiproliferative protein BTG1 (B-cell translocation gene 1). Since the protein hCAF1 (CCR4-associated factor 1) was described to interact with BTG1, we investigated a functional link between hCAF1 and PRMT1. By co-immunoprecipitation and immunofluorescence experiments we demonstrated that endogenous hCAF1 and PRMT1 interact in vivo and colocalize in nuclear speckles, a sub-nuclear compartment enriched in small nuclear ribonucleoproteins and splicing factors. In vitro methylation assays indicated that hCAF1 is not a substrate for PRMT1-mediated methylation, but it regulates PRMT1 activity in a substrate-dependent manner. Moreover, small interfering RNA (siRNA)-mediated silencing of hCAF1 in MCF-7 cells significantly modulates the methylation of endogenous PRMT1 substrates. Finally, we demonstrated that in vitro and in the cellular context, hCAF1 regulates the methylation of Sam68 and histone H4, two PRMT1 substrates. Since hCAF1 and PRMT1 have been involved in the regulation of transcription and RNA metabolism, we speculate that hCAF1 and PRMT1 could contribute to the crosstalk between transcription and RNA processing.
    Document Type:
    Reference
    Product Catalog Number:
    Multiple
    Product Catalog Name:
    Multiple

  • Five friends of methylated chromatin target of protein-arginine-methyltransferase[prmt]-1 (chtop), a complex linking arginine methylation to desumoylation. 22872859

    Chromatin target of Prmt1 (Chtop) is a vertebrate-specific chromatin-bound protein that plays an important role in transcriptional regulation. As its mechanism of action remains unclear, we identified Chtop-interacting proteins using a biotinylation-proteomics approach. Here we describe the identification and initial characterization of Five Friends of Methylated Chtop (5FMC). 5FMC is a nuclear complex that can only be recruited by Chtop when the latter is arginine-methylated by Prmt1. It consists of the co-activator Pelp1, the Sumo-specific protease Senp3, Wdr18, Tex10, and Las1L. Pelp1 functions as the core of 5FMC, as the other components become unstable in the absence of Pelp1. We show that recruitment of 5FMC to Zbp-89, a zinc-finger transcription factor, affects its sumoylation status and transactivation potential. Collectively, our data provide a mechanistic link between arginine methylation and (de)sumoylation in the control of transcriptional activity.
    Document Type:
    Reference
    Product Catalog Number:
    Multiple
    Product Catalog Name:
    Multiple

  • Smart Up your lab

    Document Type:
    Brochure
    Product Catalog Number:
    Multiple
    Product Catalog Name:
    Multiple

  • More Than Sure

    Document Type:
    Brochure
    Product Catalog Number:
    Multiple
    Product Catalog Name:
    Multiple