精氨酸甲基转移酶及其生物学功能研究进展

摘要/Abstract

摘要： 精氨酸甲基转移酶在蛋白质转录后修饰中起着重要作用。最近的研究进展揭示精氨酸甲基转移酶在真核生物的生长、发育及适应过程中起着非常重要作用。然而人们对该类酶功能和参与调控机制的认识还很少。该文综述了精氨酸甲基转移酶的分类标准、各种类型精氨酸甲基转移酶的生化特性及在动物、植物和酵母中精氨酸甲基转移酶的种类。分析了精氨酸甲基转移酶蛋白质结构特征及作用底物的特点。并综述了最近动植物中精氨酸甲基转移酶功能研究的进展，精氨酸甲基转移酶的生物学功能研究进展及其活性的调控方式；并对进一步研究精氨酸甲基转移酶功能进行了展望。

关键词: 莲（Nelumbo nucifera Gaertn）, 莲（Nelumbo nucifera Gaertn）, 克隆构型

Abstract: Arginine methyltranserases play very important roles in protein post-translational modification. Recent progresses have shown that the arginine methyltranserases regulate growth and development of eukaryotes, and are involved in adaptation to their environment. However, the functions of these enzymes and the underlying molecular mechanisms are largely unknown. In this review, we describe the classification and the structures of the arginine methyltranserses. We also summarize the recent progresses in the functions of arginine methyltransferases in plants and animals. Finally, we present our outlook for the future and discuss directions of future research in the functional study of arginine methyltransferases.

中图分类号:

王丽丽, ,朱祯,李霞. 精氨酸甲基转移酶及其生物学功能研究进展[J]. 中国农学通报, 2008, 24(7): 39-44.

Wang Lili, , Zhu Zhen, Li Xia. Advances in Arginine Methyltransferases and their Functions[J]. Chinese Agricultural Science Bulletin, 2008, 24(7): 39-44.

参考文献

[1] Bedford M T. Arginine methylation at a glance. Journal of cell science, 2007, 120: 4243-4246.
[2] Paik W K , Kim S. Enzymatic methylation of protein fractions from calf thymus nuclei. Biochemical and biophysical research communications, 1967, 29: 14-20.
[3] Bedford M T , Richard S. Arginine methylation an emerging regulator of protein function. Molecular cell, 2005, 18: 263-272.
[4] Gary J D, Lin W J, Yang M C, et al. The predominant protein-arginine methyltransferase from Saccharomyces cerevisiae. The Journal of biological chemistry ,1996, 271: 12585-12594.
[5] Katz J E, Dlakic M ,Clarke S. Automated identification of putative methyltransferases from genomic open reading frames. Mol Cell Proteomics,2003, 2: 525-540.
[6] Gary J D , Clarke S. RNA and protein interactions modulated by protein arginine methylation. Progress in nucleic acid research and molecular biology. 1998, 61: 65-131.
[7] Boisvert F M., Chénard C A, Richard S. Protein Interfaces in Signaling Regulated by Arginine Methylation. Science STKE, 2005, 271: 2.
[8] Cook J R, Lee J-H, Yang Z-H, et al. FBXO11/PRMT9, a new protein arginine methyltransferase, symmetrically dimethylates arginine residues. Biochemical and Biophysical Research Communications, 2006a, 342: 472-481.
[9] Krause C D, Yang Z-H, Kim Y-S, et al. Protein arginine methyltransferases: Evolution and assessment of their pharmacological and therapeutic potential. Pharmacology & Therapeutics,2007,113: 50-87.
[10] Scott H S, Antonarakis S E, Lalioti M D, et al. Identification and characterization of two putative human arginine methyltransferases (HRMT1L1 and HRMT1L2). Genomics, 1998, 48: 330-340.
[11] Thomas R. Cimato J. Nerve growth factor-mediated increases in protein methylation occur predominantly at type I arginine methylation sites and involve protein arginine methyltransferase 1. Journal of Neuroscience Research, 2002, 67: 435-442.
[12] Zobel-Thropp P, Gary J D , Clarke S. delta -N-Methylarginine Is a Novel Posttranslational Modification of Arginine Residues in Yeast Proteins. J. Biol. Chem, 1998, 273: 29283-29286.
[13] Pei Y, Niu L, Lu F, et al. Mutations in the Type II protein arginine methyltransferase AtPRMT5 result in pleiotropic developmental defects in Arabidopsis. Plant Physiol ,2007, 144: 1913-1923.
[14] Wang X, Zhang Y, Ma Q, et al. SKB1-mediated symmetric dimethylation of histone H4R3 controls flowering time in Arabidopsis. The EMBO journal, 2007, 26: 1934-1941.
[15] Niu L, Lu F, Pei Y, Liu C et al. Regulation of flowering time by the protein arginine methyltransferase AtPRMT10. EMBO Rep, 2007, 8:1190-1195.
[16] Niewmierzycka A and Clarke S. S-Adenosylmethionine-dependent methylation in Saccharomyces cerevisiae. Identification of a novel protein arginine methyltransferase. The Journal of biological chemistry,1999, 274: 814-824.
[17] Zhang X, Zhou L , Cheng X. Crystal structure of the conserved core of protein arginine methyltransferase PRMT3. The EMBO journal, 2000, 19: 3509-3519.
[18] Cheng, D., Cote, J., Shaaban, S. and Bedford, M. T. The arginine methyltransferase CARM1 regulates the coupling of transcription and mRNA processing. Molecular Cell, 2007, 25:71-83.
[19] Lin W J, Gary J D, Yang M C, et al. The mammalian immediate-early TIS21 protein and the leukemia-associated BTG1 protein interact with a protein-arginine N-methyltransferase. The Journal of biological chemistry, 1996, 271:15034-15044.
[20] Pawlak M R, Scherer C A, Chen J, et al. Arginine N-methyltransferase 1 is required for early postimplantation mouse development, but cells deficient in the enzyme are viable. Molecular and cellular biology, 2000, 20: 4859-4869.
[21] Tang J, Gary J D, Clarke S et al. PRMT 3, a type I protein arginine N-methyltransferase that differs from PRMT1 in its oligomerization, subcellular localization, substrate specificity, and regulation. The Journal of biological chemistry,1998, 273:16935-16945.
[22] Tang J, Kao P N , Herschman H R. Protein-arginine Methyltransferase I, the Predominant Protein-arginine Methyltransferase in Cells, Interacts with and Is Regulated by Interleukin Enhancer-binding Factor 3. J. Biol. Chem, 2000, 275: 19866-19876.
[23] Qi C, Chang J, Zhu Y, et al. Identification of protein arginine methyltransferase 2 as a coactivator for estrogen receptor alpha. The Journal of biological chemistry, 2000, 277: 28624-28630.
[24] Ganesh L, Yoshimoto T, Moorthy N C, et al. Protein methyltransferase 2 inhibits NF-kappaB function and promotes apoptosis. Molecular and cellular biology, 2006, 26: 3864-3874.
[25] Swiercz R, Cheng D, Kim D, et al. Ribosomal Protein rpS2 Is Hypomethylated in PRMT3-deficient Mice. J. Biol. Chem, 2007, 282:16917-16923.
[26] Chen D, Huang S-M , Stallcup M R. Synergistic, p160 Coactivator-dependent Enhancement of Estrogen Receptor Function by CARM1 and p300. J. Biol. Chem, 2000, 275: 810-40816.
[27] Kim J, Lee J, Yadav N, et al. Loss of CARM1 results in hypomethylation of thymocyte cyclic AMP-regulated phosphoprotein and deregulated early T cell development. The Journal of biological chemistry, 2004, 279: 25339-25344.
[28] Pollack B P, Kotenko S V, He W, et al. The Human Homologue of the Yeast Proteins Skb1 and Hsl7p Interacts with Jak Kinases and Contains Protein Methyltransferase Activity. J. Biol. Chem, 1999, 274:31531-31542.
[29] Branscombe T L, Frankel A, Lee J-H, et al. PRMT5 (Janus Kinase-binding Protein 1) Catalyzes the Formation of Symmetric Dimethylarginine Residues in Proteins. J. Biol. Chem, 2001, 276:32971-32976.
[30] Lee J-H, Cook J R, Yang Z-H, et al. PRMT7, a New Protein Arginine Methyltransferase That Synthesizes Symmetric Dimethylarginine. J. Biol. Chem, 2005, 280: 3656-3664.
[31] Rho J, Choi S, Seong Y R, et al. The Arginine-1493 Residue in QRRGRTGR1493G Motif IV of the Hepatitis C Virus NS3 Helicase Domain Is Essential for NS3 Protein Methylation by the Protein Arginine Methyltransferase 1. J. Virol. 2001, 75: 8031-8044.
[32] Miranda T B, Webb K J, Edberg D D, et al. Protein arginine methyltransferase 6 specifically methylates the nonhistone chromatin protein HMGA1a. Biochemical and biophysical research communications, 2005, 336: 831-835.
[33] Frankel A, Yadav N, Lee J, et al. The Novel Human Protein Arginine N-Methyltransferase PRMT6 Is a Nuclear Enzyme Displaying Unique Substrate Specificity. J. Biol. Chem, 2002, 277: 3537-3543.
[34] Miranda T B, Miranda M, Frankel A ,et al. PRMT7 Is a Member of the Protein Arginine Methyltransferase Family with a Distinct Substrate Specificity. J. Biol. Chem. 2004, 279: 902-22907.
[35] Gros L, Delaporte C, Frey S, et al. Identification of New Drug Sensitivity Genes Using Genetic Suppressor Elements: Protein Arginine N-Methyltransferase Mediates Cell Sensitivity to DNA-damaging Agents. Cancer Res,2003, 63: 164-171.
[36] Zheng Z, Schmidt-Ott K M, Chua S, et al. A Mendelian locus on chromosome 16 determines susceptibility to doxorubicin nephropathy in the mouse. Proceedings of the National Academy of Sciences, 2005, 102: 2502-2507.
[37] Lee J, Sayegh J, Daniel J, et al. PRMT8, a New Membrane-bound Tissue-specific Member of the Protein Arginine Methyltransferase Family. J. Biol. Chem, 2005, 280: 32890-32896.
[38] Pahlich S, Zakaryan RP, Gehring H.Protein arginine methylation: Cellular functions and methods of analysis. Biochim Biophys Acta, 2006, 1764:1890-1903.
[39] Zhang Y , Reinberg D. Transcription regulation by histone methylation: interplay between different covalent modifications of the core histone tails. Genes Dev, 2001, 15: 2343-2360.
[40] McBride A E , Silver P A. State of the Arg: Protein Methylation at Arginine Comes of Age. Cell, 2001, 106: 5-8.
[41] Pal S, Vishwanath S N, Erdjument-Bromage H, et al. Human SWI/SNF-Associated PRMT5 Methylates Histone H3 Arginine 8 and Negatively Regulates Expression of ST7 and NM23 Tumor Suppressor Genes. Mol. Cell. Biol, 2004, 24: 9630-9645.
[42] Chevillard-Briet M, Trouche D , Vandel L. Control of CBP co-activating activity by arginine methylation. The EMBO journal, 2002, 21: 5457-5466.
[43] Kwak Y T, Guo J, Prajapati S, et al. Methylation of SPT5 regulates its interaction with RNA polymerase II and transcriptional elongation properties. Molecular cell, 2003, 11:1055-1066.
[44] Boisvert F M, Hendzel M J, Masson J Y et al. Methylation of MRE11 regulates its nuclear compartmentalization. Cell cycle (Georgetown), 2005, 4: 981-989.
[45] Adams M M, Wang B, Xia Z, et al. 53BP1 oligomerization is independent of its methylation by PRMT1. Cell cycle (Georgetown), 2005,4: 1854-1861.
[46] Boisvert F M, Rhie A, Richard S et al. The GAR motif of 53BP1 is arginine methylated by PRMT1 and is necessary for 53BP1 DNA binding activity. Cell cycle (Georgetown), 2005, 4:1834-1841.
[47] Robin-Lespinasse Y, Sentis S, Kolytcheff C, et al. hCAF1, a new regulator of PRMT1-dependent arginine methylation. Journal of cell science, 2007, 120: 638-647.
[48] Singh V, Miranda T B, Jiang W, et al. DAL-1//4.1B tumor suppressor interacts with protein arginine N-methyltransferase 3 (PRMT3) and inhibits its ability to methylate substrates in vitro and in vivo. Oncogene, 2004, 23: 7761-7771.
[49] Xu W, Cho H, Kadam S, et al. A methylation-mediator complex in hormone signaling. Genes & development, 2004, 18: 144-156.
[50] Jelinic P, Stehle J-C , Shaw P. The Testis-Specific Factor CTCFL Cooperates with the Protein Methyltransferase PRMT7 in H19 Imprinting Control Region Methylation. PLoS Biology, 2006, 4: 355.