Identification and Characterization of Two New S-Adenosylmethionine- Dependent Methyltransferase Encoding Genes Suggested Their Involvement in Stipe Elongation of Flammulina velutipes = Identification and Characterization of Two New S-Adenosylmethionine- Dependent Methyltransferase Encoding Genes Suggested Their Involvement in Stipe Elongation of Flammulina velutipes

다국어 초록 (Multilingual Abstract)

Two new SAM-dependent methyltransferase encoding genes (fvsmt1 and fvsmt2) were identified from the genome of Flammulina velutipes. In order to make a comprehensive characterization of both genes, we performed in silico analysis of both genes and used qRT-PCR to reveal their expression patterns during the development of F. velutipes. There are 4 and 6 exons with total length of 693 and 978 bp in fvsmt2 and fvsmt1, respectively. The deduced proteins, i.e., FVSMT1 and FVSMT2 contained 325 and 230 amino acids with molecular weight 36297 and 24894 Da, respectively. Both proteins contained a SAM-dependent catalytic domain with signature motifs (I, p-I, II, and III) defining the SAM fold. SAM-dependent catalytic domain is located either in the middle or at the N-terminal of FVSMT2 and FVSMT1, respectively. Alignment and phylogenic analysis showed that FVSMT1 is a homolog to a protein- arginine omega-N-methyltransferase, while FVSMT2 is of cinnamoyl CoA O-methyltransferase type and predicted subcellular locations of these proteins are mitochondria and cytoplasm, respectively. qRT-PCR showed that fvsmt1 and fvsmt2 expression was regulated in different developmental stages. The maximum expression levels of fvsmt1 and fvsmt2 were observed in stipe elongation, while no difference was found in mycelium and pileus. These results positively demonstrate that both the methyltransferase encoding genes are involved in the stipe elongation of F. velutipes.

참고문헌 (Reference)

1 Kagan RM, "Widespread occurrence of three sequence motifs in diverse S-adenosylmethionine-dependent methyltransferases suggests a common structure for these enzymes" 310 : 417-427, 1994

2 Weng JK, "The origin and evolution of lignin biosynthesis" 187 : 273-285, 2010

3 Saitou N, "The neighbor-joining method : a new method for reconstructing phylogenetic trees" 4 : 406-425, 1987

4 Dekkers KL, "The Cercospora nicotianae gene encoding dual O-methyltransferase and FAD-dependent monooxygenase domains mediates cercosporin toxin biosynthesis" 44 : 444-454, 2007

5 Yoneyama N, "Substrate specificity of N-methyltransferase involved in purine alkaloids synthesis is dependent upon one amino acid residue of the enzyme" 275 : 125-135, 2006

6 Patnaik D, "Substrate specificity and kinetic mechanism of mammalian G9a histone H3 methyltransferase" 279 : 53248-53258, 2004

7 Zubieta C, "Structures of two natural product methyltransferases reveal the basis for substrate specificity in plant O-methyltransferases" 8 : 271-279, 2001

8 Lam KC, "Structure, function, and evolution of plant O-methyltransferases" 50 : 1001-1013, 2007

9 Ho MC, "Structure of the arginine methyltransferase PRMT5-MEP50reveals a mechanism for substrate specificity" 8 : e57008-, 2013

10 Zubieta C, "Structural basis for substrate recognition in the salicylic acid carboxyl methyltransferase family" 15 : 1704-1716, 2003

11 Fang H, "Stipe wall extension of Flammulina velutipes could be induced by an expansin-like protein from Helix aspersa" 118 : 1-11, 2014

12 Ramamoorthy V, "Sphingolipid C-9 methyltransferases are important for growth and virulence but not for sensitivity to antifungal plant defensins in Fusarium graminearum" 8 : 217-229, 2009

13 Xiao B, "Specificity and mechanism of the histone methyltransferase Pr-Set7" 19 : 1444-1454, 2005

14 Struck AW, "S-adenosyl-methionine-dependent methyltransferases : highly versatile enzymes in biocatalysis, biosynthesis and other biotechnological applications" 13 : 2642-2655, 2012

15 Zhang X, "Regulation of estrogen receptor a by histone methyltransferase SMYD2-mediated protein methylation" 110 : 17284-17289, 2013

16 Miranda TB, "PRMT7is a member of the protein arginine methyltransferase family with a distinct substrate specificity" 279 : 22902-22907, 2004

17 Tang J, "PRMT 3, a type I protein arginine N-methyltransferase that differs from PRMT1 in its oligomerization, subcellular localization, substrate specificity, and regulation" 273 : 16935-16945, 1998

18 Yang DCH, "Outer membrane protein OmpB methylation may mediate bacterial virulence" 42 : 936-945, 2017

19 Sarikaya-Bayram O, "One Juliet and four Romeos : VeA and its methyltransferases" 6 : 1-, 2015

20 Shields DJ, "Molecular dissection of the S-adenosylmethionine-binding site of phosphatidylethanolamine N-methyltransferase" 278 : 35826-35836, 2003

21 Li W, "Molecular cloning and characterization of juvenile hormone acid methyltransferase in the honey bee, Apis mellifera, and its differential expression during caste differentiation" 8 : e68544-, 2013

22 Fischer JA, "Methylation is involved in the Ustilago maydis mating response" 34 : 21-35, 2001

23 Sarikaya-Bayram O, "Membrane-bound methyltransferase complex VapA-VipC-VapB guides epigenetic control of fungal development" 29 : 406-420, 2014

24 Kumar S, "MEGA7: molecular evolutionary genetics analysis version 7.0for bigger datasets" 33 : 1870-1874, 2016

25 Boerjan W, "Lignin biosynthesis" 54 : 519-546, 2003

26 Wang J, "Identification of specific residues involved in substrate discrimination in two plant O-methyltransferases" 368 : 172-180, 1999

27 Tao Y, "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" 527 : 154-160, 2013

28 Qianhui Huang, "Identification and Expression Patterns of fvexpl1, an Expansin-Like Protein-Encoding Gene, Suggest an Auxiliary Role in the Stipe Morphogenesis of Flammulina velutipes" 한국미생물·생명공학회 28 (28): 622-629, 2018

29 Yang XJ, "Gene body methylation can alter gene expression and is a therapeutic target in cancer" 26 : 577-590, 2014

30 Dunn J, "Flow-dependent epigenetic DNA methylation regulates endothelial gene expression and atherosclerosis" 124 : 3187-3199, 2014

31 Martienssen RA, "DNA methylation and epigenetic inheritance in plants and filamentous fungi" 293 : 1070-1074, 2001

32 Smith ZD, "DNA methylation : roles in mammalian development" 14 : 204-220, 2013

33 Vermillion KL, "Cytoplasmic protein methylation is essential for neural crest migration" 204 : 95-109, 2014

34 Alvarez-Rodriguez ML, "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" 68 : 5860-5869, 2002

35 Wlodarski T, "Comprehensive structural and substrate specificity classification of the Saccharomyces cerevisiae methyltransferome" 6 : e23168-, 2011

36 Yamada M, "Cloning and characterization of a gene coding for a hydrophobin, Fv-hyd1, specifically expressed during fruiting body development in the basidiomycete Flammulina velutipes" 67 : 240-246, 2005

37 Yu J, "Cloning and characterization of a cDNA from Aspergillus parasiticus encoding an O-methyltransferase involved in aflatoxin biosynthesis" 59 : 3564-3571, 1993

38 Nagatoshi Y, "Characterization of three halide methyltransferases in Arabidopsis thaliana" 24 : 503-506, 2007

39 Coque JJR, "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" 69 : 5089-5095, 2003

40 Bedford MT, "Arginine methylation an emerging regulator of protein function" 18 : 263-272, 2005