참고문헌
- Martienssen RA, Colot V. DNA methylation and epigenetic inheritance in plants and filamentous fungi. Science. 2001;293:1070-1074. https://doi.org/10.1126/science.293.5532.1070
- Bedford MT, Richard S. Arginine methylation an emerging regulator of protein function. Mol Cell. 2005;18:263-272. https://doi.org/10.1016/j.molcel.2005.04.003
- Wlodarski T, Kutner J, Towpik J, et al. Comprehensive structural and substrate specificity classification of the Saccharomyces cerevisiae methyltransferome. PLoS One. 2011;6:e23168. https://doi.org/10.1371/journal.pone.0023168
- Smith ZD, Meissner A. DNA methylation: roles in mammalian development. Nat Rev Genet. 2013;14:204-220. https://doi.org/10.1038/nrg3354
- Dunn J, Qiu HW, Kim S, et al. Flow-dependent epigenetic DNA methylation regulates endothelial gene expression and atherosclerosis. J Clin Invest. 2014;124:3187-3199. https://doi.org/10.1172/jci74792
- Yang XJ, Han H, De Carvalho DD, et al. Gene body methylation can alter gene expression and is a therapeutic target in cancer. Cancer Cell. 2014;26:577-590. https://doi.org/10.1016/j.ccr.2014.07.028
- Vermillion KL, Lidberg KA, Gammill LS. Cytoplasmic protein methylation is essential for neural crest migration. J Cell Biol. 2014;204:95-109. https://doi.org/10.1083/jcb.201306071
- Yang DCH, Abeykoon AH, Choi BE, et al. Outer membrane protein OmpB methylation may mediate bacterial virulence. Trends Biochem Sci. 2017;42:936-945. https://doi.org/10.1016/j.tibs.2017.09.005
- Zhang X, Tanaka K, Yan JS, et al. Regulation of estrogen receptor a by histone methyltransferase SMYD2-mediated protein methylation. Proc Natl Acad Sci USA. 2013;110:17284-17289. https://doi.org/10.1073/pnas.1307959110
- Struck AW, Thompson ML, Wong LS, et al. S-adenosyl-methionine-dependent methyltransferases: highly versatile enzymes in biocatalysis, biosynthesis and other biotechnological applications. Chembiochem. 2012;13:2642-2655. https://doi.org/10.1002/cbic.201200556
- Yu J, Cary JW, Bhatnagar D, et al. Cloning and characterization of a cDNA from Aspergillus parasiticus encoding an O-methyltransferase involved in aflatoxin biosynthesis. Appl Environ Microbiol. 1993;59:3564-3571. https://doi.org/10.1128/aem.59.11.3564-3571.1993
- Dekkers KL, You BJ, Gowda VS, et al. The Cercospora nicotianae gene encoding dual O-methyltransferase and FAD-dependent monooxygenase domains mediates cercosporin toxin biosynthesis. Fungal Genet Biol. 2007;44:444-454. https://doi.org/10.1016/j.fgb.2006.08.005
- Alvarez-Rodriguez ML, Lopez-Ocana L, Lopez-Coronado JM, et al. Cork taint of wines: role of the filamentous fungi isolated from cork in the formation of 2,4,6-trichloroanisole by O methylation of 2,4,6-trichlorophenol. Appl Environ Microbiol. 2002;68:5860-5869. https://doi.org/10.1128/AEM.68.12.5860-5869.2002
- Coque JJR, Alvarez-Rodriguez ML, Larriba G. Characterization of an inducible chlorophenol Omethyltransferase from trichoderma longibrachiatum involved in the formation of chloroanisoles and determination of its role in cork taint of wines. Appl Environ Microbiol. 2003;69:5089-5095. https://doi.org/10.1128/AEM.69.9.5089-5095.2003
- Ramamoorthy V, Cahoon EB, Thokala M, et al. Sphingolipid C-9 methyltransferases are important for growth and virulence but not for sensitivity to antifungal plant defensins in Fusarium graminearum. Eukaryot Cell. 2009;8:217-229. https://doi.org/10.1128/EC.00255-08
- Weng JK, Chapple C. The origin and evolution of lignin biosynthesis. New Phytol. 2010;187:273-285. https://doi.org/10.1111/j.1469-8137.2010.03327.x
- Fischer JA, McCann MP, Snetselaar KM. Methylation is involved in the Ustilago maydis mating response. Fungal Genet Biol. 2001;34:21-35. https://doi.org/10.1006/fgbi.2001.1287
- Sarikaya-Bayram O, Bayram O, Feussner K, et al. Membrane-bound methyltransferase complex VapA-VipC-VapB guides epigenetic control of fungal development. Dev Cell. 2014;29:406-420. https://doi.org/10.1016/j.devcel.2014.03.020
- Sarikaya-Bayram O, Palmer JM, Keller N, et al. One Juliet and four Romeos: VeA and its methyltransferases. Front Microbiol. 2015;6:1. https://doi.org/10.3389/fmicb.2015.00001
- Saitou N, Nei M. The neighbor-joining method: a new method for reconstructing phylogenetic trees. Mol Biol Evol. 1987;4:406-425.
- Kumar S, Stecher G, Tamura K. MEGA7: molecular evolutionary genetics analysis version 7.0 for bigger datasets. Mol Biol Evol.. 2016;33:1870-1874. https://doi.org/10.1093/molbev/msw054
- Lam KC, Ibrahim RK, Behdad B, et al. Structure, function, and evolution of plant O-methyltransferases. Genome. 2007;50:1001-1013. https://doi.org/10.1139/G07-077
- Yamada M, Sakuraba S, Shibata K, et al. Cloning and characterization of a gene coding for a hydrophobin, Fv-hyd1, specifically expressed during fruiting body development in the basidiomycete Flammulina velutipes. Appl Microbiol Biotechnol. 2005;67:240-246. https://doi.org/10.1007/s00253-004-1776-2
- Fang H, Zhang W, Niu X, et al. Stipe wall extension of Flammulina velutipes could be induced by an expansin-like protein from Helix aspersa. Fungal Biol. 2014;118:1-11. https://doi.org/10.1016/j.funbio.2013.10.003
- Huang Q, Han X, Mukhtar I, et al. Identification and expression patterns of fvexpl1, an expansinlike protein-encoding gene, suggest an auxiliary role in the stipe morphogenesis of Flammulina velutipes. J Microbiol Biotechnol. 2018;28:622-629. https://doi.org/10.4014/jmb.1712.12046
- Tao Y, Xie B, Yang Z, et al. Identification and expression analysis of a new glycoside hydrolase family 55 exo-beta-1,3-glucanase-encoding gene in Volvariella volvacea suggests a role in fruiting body development. Gene. 2013;527:154-160. https://doi.org/10.1016/j.gene.2013.05.071
- Kagan RM, Clarke S. Widespread occurrence of three sequence motifs in diverse S-adenosylmethionine-dependent methyltransferases suggests a common structure for these enzymes. Arch Biochem Biophys. 1994;310:417-427. https://doi.org/10.1006/abbi.1994.1187
- Shields DJ, Altarejos JY, Wang X, et al. Molecular dissection of the S-adenosylmethionine-binding site of phosphatidylethanolamine N-methyltransferase. J Biol Chem. 2003;278:35826-35836. https://doi.org/10.1074/jbc.M306308200
- Tang J, Gary JD, 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. J Biol Chem. 1998;273:16935-16945. https://doi.org/10.1074/jbc.273.27.16935
- Miranda TB, 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;279:22902-22907. https://doi.org/10.1074/jbc.M312904200
- Patnaik D, Chin HG, Esteve PO, et al. Substrate specificity and kinetic mechanism of mammalian G9a histone H3 methyltransferase. J Biol Chem. 2004;279:53248-53258. https://doi.org/10.1074/jbc.M409604200
- Xiao B, Jing C, Kelly G, et al. Specificity and mechanism of the histone methyltransferase Pr-Set7. Genes Dev. 2005;19:1444-1454. https://doi.org/10.1101/gad.1315905
- Wang J, Pichersky E. Identification of specific residues involved in substrate discrimination in two plant O-methyltransferases. Arch Biochem Biophys. 1999;368:172-180. https://doi.org/10.1006/abbi.1999.1304
- Zubieta C, He XZ, Dixon RA, et al. Structures of two natural product methyltransferases reveal the basis for substrate specificity in plant O-methyltransferases. Nat Struct Biol. 2001;8:271-279. https://doi.org/10.1038/85029
- Zubieta C, Ross JR, Koscheski P, et al. Structural basis for substrate recognition in the salicylic acid carboxyl methyltransferase family. Plant Cell. 2003;15:1704-1716. https://doi.org/10.1105/tpc.014548
- Yoneyama N, Morimoto H, Ye CX, et al. Substrate specificity of N-methyltransferase involved in purine alkaloids synthesis is dependent upon one amino acid residue of the enzyme. Mol Genet Genomics. 2006;275:125-135. https://doi.org/10.1007/s00438-005-0070-z
- Ho MC, Wilczek C, Bonanno JB, et al. Structure of the arginine methyltransferase PRMT5-MEP50 reveals a mechanism for substrate specificity. PLoS One. 2013;8:e57008. https://doi.org/10.1371/journal.pone.0057008
- Boerjan W, Ralph J, Baucher M. Lignin biosynthesis. Annu Rev Plant Biol. 2003;54:519-546. https://doi.org/10.1146/annurev.arplant.54.031902.134938
- Nagatoshi Y, Nakamura T. Characterization of three halide methyltransferases in Arabidopsis thaliana. Plant Biotechnol. 2007;24:503-506. https://doi.org/10.5511/plantbiotechnology.24.503
- Li W, Huang ZY, Liu F, et al. Molecular cloning and characterization of juvenile hormone acid methyltransferase in the honey bee, Apis mellifera, and its differential expression during caste differentiation. PLoS One. 2013;8:e68544. https://doi.org/10.1371/journal.pone.0068544
피인용 문헌
- Proteomic analysis of the inhibitory effect of the butanolic fraction of Jacquinia macrocarpa on Fusarium verticillioides vol.66, pp.10, 2019, https://doi.org/10.1139/cjm-2020-0127