Expression pattern of prmt5 in adult fish and embryos of medaka, Oryzias latipes

被引:15
作者
Chen, W. [1 ]
Cao, M. [1 ]
Yang, Y. [1 ]
Nagahama, Y. [2 ]
Zhao, H. [1 ]
机构
[1] Huazhong Normal Univ, Sch Life Sci, Hubei Key Lab Genet Regulat & Integrat Biol, Wuhan 430079, Peoples R China
[2] Natl Inst Basic Biol, Okazaki, Aichi 4448585, Japan
关键词
Embryogenesis; Expression pattern; Germ cells; Medaka; Oryzias latipes; prmt5; Protein arginine methyltransferase; ARGININE METHYLTRANSFERASE PRMT5; PRIMORDIAL GERM-CELLS; PROTEIN METHYLTRANSFERASE; GENE; METHYLATION; DOMAIN; IDENTIFICATION; SPECIFICATION; FAMILY; BLIMP1;
D O I
10.1007/s10695-008-9233-2
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
DNA methylation is an important biochemical epigenetic determinant of gene expression in cells and therefore actively involved in gene regulation, chromosomal conformation, and protein activity. Protein arginine methyltransferases (PRMTs) play a major role in the methylation of proteins that have an arginine residue, catalyzing both the asymetric dimethylation of arginine (aDMA) and symetric dimethylation of arginine (sDMA). PRMT5, a type II PRMT which catalyzes sDMA, has been shown to have a pivotal role in pole plasm assembly and germ cell development in Drosophila and also to be an associate factor of Blimp1 for germ cell development in mouse. Here, we report a homolog of prmt5 identified in medaka, Oryzias latipes, which was detected in the brain, gill, muscle, heart, liver, spleen, intestine, testis and ovary of adult fish by reverse transcriptase-PCR. The expression of prmt5 in the gonads is restricted to oocytes of the ovary, spermatogonia, and spermatocytes of testis. The prmt5 transcripts were detected as early as the one-cell stage and in all the tissues of embryos during embryogenesis. In summary, prmt5 is a maternal determinant factor of embryogenesis of medaka, possibly playing an important role in oogenesis and spermatogenesis in adult medaka.
引用
收藏
页码:325 / 332
页数:8
相关论文
共 28 条
[1]   A protein-arginine methyltransferase binds to the intracytoplasmic domain of the IFNAR1 chain in the type I interferon receptor [J].
Abramovich, C ;
Yakobson, B ;
Chebath, J ;
Revel, M .
EMBO JOURNAL, 1997, 16 (02) :260-266
[2]   Involvement of receptor-bound protein methyltransferase PRMT1 in antiviral and antiproliferative effects of type I interferons [J].
Altschuler, L ;
Wook, JO ;
Gurari, D ;
Chebath, J ;
Revel, M .
JOURNAL OF INTERFERON AND CYTOKINE RESEARCH, 1999, 19 (02) :189-195
[3]   Identification of proteins interacting with RNAPII FCP1 phosphatase: FCP1 forms a complex with arginine methyltransferase PRMT5 and it is a substrate for PRMT5-mediated methylation [J].
Amente, S ;
Napolitanoa, G ;
Lieciardo, P ;
Monti, M ;
Pucci, P ;
Lania, L ;
Majello, B .
FEBS LETTERS, 2005, 579 (03) :683-689
[4]   Blimp1 associates with Prmt5 and directs histone arginine methylation in mouse germ cells [J].
Ancelin, Katia ;
Lange, Ulrike C. ;
Hajkova, Petra ;
Schneider, Robert ;
Bannister, Andrew J. ;
Kouzarides, Tony ;
Surani, M. Azim .
NATURE CELL BIOLOGY, 2006, 8 (06) :623-630
[5]   Arginine methyltransferase Capsuleen is essential for methylation of spliceosomal Sm proteins and germ cell formation in Drosophila [J].
Anne, Joel ;
Ollo, Roger ;
Ephrussi, Anne ;
Mechler, Bernard M. .
DEVELOPMENT, 2007, 134 (01) :137-146
[6]   A proteomic analysis of arginine-methylated protein complexes [J].
Boisvert, FM ;
Côté, J ;
Boulanger, MC ;
Richard, S .
MOLECULAR & CELLULAR PROTEOMICS, 2003, 2 (12) :1319-1330
[7]   The protein arginine methyltransferase Prmt5 is required for myogenesis because it facilitates ATP-dependent chromatin remodeling [J].
Dacwag, Caroline S. ;
Ohkawa, Yasuyuki ;
Pal, Sharmistha ;
Sif, Said ;
Imbalzano, Anthony N. .
MOLECULAR AND CELLULAR BIOLOGY, 2007, 27 (01) :384-394
[8]  
Eddy E.M., 2006, Encycl. Life Sci., DOI [10.1038/npg.els.0005960, DOI 10.1038/NPG.ELS.0005960]
[9]   SMN, the product of the spinal muscular atrophy gene, binds preferentially to dimethylarginine-containing protein targets [J].
Friesen, WJ ;
Massenet, S ;
Paushkin, S ;
Wyce, A ;
Dreyfuss, G .
MOLECULAR CELL, 2001, 7 (05) :1111-1117
[10]   Negative regulation of mitosis in fission yeast by the Shk1-interacting protein Skb1 and its human homolog, Skb1Hs [J].
Gilbreth, M ;
Yang, PR ;
Bartholomeusz, G ;
Pimental, RA ;
Kansra, S ;
Gadiraju, R ;
Marcus, S .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1998, 95 (25) :14781-14786