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      The PRMT1 gene expression pattern in colon cancer

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          Abstract

          The methylation of arginine has been implicated in many cellular processes, such as regulation of transcription, mRNA splicing, RNA metabolism and transport. The enzymes responsible for this modification are the protein arginine methyltransferases. The most abundant methyltransferase in human cells is protein arginine methyltransferase 1. Methylation processes appear to interfere in the emergence of several diseases, including cancer. During our study, we examined the expression pattern of protein arginine methyltransferase 1 gene in colon cancer patients. The emerging results showed that the expression of one of the gene variants is associated with statistical significant probability to clinical and histological parameters, such as nodal status and stage. This is a first attempt to acquire an insight on the possible relation of the expression pattern of protein arginine methyltransferase 1 and colon cancer progression.

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          Arginine methylation an emerging regulator of protein function.

          Mark Bedford, Stéphane Richard (2005)
          Arginine methylation is now coming out of the shadows of protein phosphorylation and entering the mainstream, largely due to the identification of the family of enzymes that lay down this modification. In addition, modification-specific antibodies and proteomic approaches have facilitated the identification of an array of substrates for the protein arginine methyltransferases. This review describes recent insights into the molecular processes regulated by arginine methylation in normal and diseased cells.
          Article 0 comments Cited 271 times – based on 0 reviews     Review now
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            Regulation of transcription by a protein methyltransferase.

            Dana W. Aswad, D Chen, Rachel S Koh … (1999)
            The p160 family of coactivators, SRC-1, GRIP1/TIF2, and p/CIP, mediate transcriptional activation by nuclear hormone receptors. Coactivator-associated arginine methyltransferase 1 (CARM1), a previously unidentified protein that binds to the carboxyl-terminal region of p160 coactivators, enhanced transcriptional activation by nuclear receptors, but only when GRIP1 or SRC-1a was coexpressed. Thus, CARM1 functions as a secondary coactivator through its association with p160 coactivators. CARM1 can methylate histone H3 in vitro, and a mutation in the putative S-adenosylmethionine binding domain of CARM1 substantially reduced both methyltransferase and coactivator activities. Thus, coactivator-mediated methylation of proteins in the transcription machinery may contribute to transcriptional regulation.
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              Methylation of histone H4 at arginine 3 facilitating transcriptional activation by nuclear hormone receptor.

              H. Wang, Z Huang, L. Xia … (2001)
              Acetylation of core histone tails plays a fundamental role in transcription regulation. In addition to acetylation, other posttranslational modifications, such as phosphorylation and methylation, occur in core histone tails. Here, we report the purification, molecular identification, and functional characterization of a histone H4-specific methyltransferase PRMT1, a protein arginine methyltransferase. PRMT1 specifically methylates arginine 3 (Arg 3) of H4 in vitro and in vivo. Methylation of Arg 3 by PRMT1 facilitates subsequent acetylation of H4 tails by p300. However, acetylation of H4 inhibits its methylation by PRMT1. Most important, a mutation in the S-adenosyl-l-methionine-binding site of PRMT1 substantially crippled its nuclear receptor coactivator activity. Our finding reveals Arg 3 of H4 as a novel methylation site by PRMT1 and indicates that Arg 3 methylation plays an important role in transcriptional regulation.
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                Author and article information

                Journal
                Journal ID (nlm-ta): Br J Cancer
                Title: British Journal of Cancer
                Publisher: Nature Publishing Group
                ISSN (Print): 0007-0920
                ISSN (Electronic): 1532-1827
                Publication date (Electronic): 09 December 2008
                Publication date (Print): 09 December 2008
                Volume: 99
                Issue: 12
                Pages: 2094-2099
                Affiliations
                [1 ]Department of Cellular Physiology, ‘G Papanicolaou' Research Center of Oncology, ‘Saint Savvas' Hospital 171 Alexandras Avenue, Athens 11522, Greece
                [2 ]Department of Gastroenterology, ‘Saint Savvas' Hospital 171 Alexandras Avenue, Athens 11522, Greece
                [3 ]Department of Biochemistry and Molecular Biology, Faculty of Biology, University of Athens Panepistimioupoli, Athens 15711, Greece
                [4 ]Department of Pathology, School of Medicine, University of Ioannina Ioannina 45110, Greece
                Author notes
                [* ]Author for correspondence: talieri@ 123456agsavvas-hosp.gr
                [5]

                These authors contributed equally to this work.

                Article
                Publisher Item ID: 6604807
                DOI: 10.1038/sj.bjc.6604807
                PMC ID: 2607217
                PubMed ID: 19078953
                SO-VID: f658f440-1870-4f1a-a68c-5f2fc06d8335
                Copyright © Copyright 2008, Cancer Research UK
                History
                Date received : 12 August 2008
                Date revision received : 10 October 2008
                Date accepted : 11 November 2008
                Categories
                Subject: Genetics and Genomics

                ScienceOpen disciplines: Oncology & Radiotherapy
                Keywords: prognosis,colon cancer,prmt1,protein arginine methyltransferase
                Data availability:
                ScienceOpen disciplines: Oncology & Radiotherapy
                Keywords: prognosis, colon cancer, prmt1, protein arginine methyltransferase

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