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Molecular cloning and characterization of C1 tetrahydrofolate (C1-THF) synthase in Bombyx mori, silkworm.
Gene. 2018 Jul 15; 663:25-33.GENE

Abstract

Folate metabolism pathway is mainly associated with syntheses of nucleic acids and proteins as well as DNA methylation and repair. Cytoplasmic C1 tetrahydrofolate (C1-THF) synthase is a central enzyme in folate metabolism and plays an important role in C1-THF conversion. The full-length sequence of silkworm (Bombyx mori) cytoplasmic C1-THF synthase (BmC1-THF synthase) gene including an open reading frame (ORF) of 932 amino acid residues was cloned. Phylogenetic analysis indicated that BmC1-THF synthase shares 84% and 81% identity with C1-THF synthase of Papilio Xuthus and Danaus plexippus, respectively. Conserved sequence analysis showed that the 330 to 710 amino acid residues of BmC1-THF synthase were highly conserved among various organisms. Recombinant BmC1-THF synthase protein with a molecular weight of about 105.5 kDa was expressed in E. coli cells and identified using SDS-PAGE and western blot analysis. The expression of BmC1-THF synthase gene in eight silkworm tissues revealed that BmC1-THF synthase gene is widely expressed in various tissues of silkworm and highly expressed in the fat body. The expression characteristics of BmC1-THF synthase gene in response to oxidative stress were conducted under phoxim and high temperature (30 °C) exposure. The results showed that the transcriptional level of BmC1-THF synthase gene was upregulated by 3.435-fold and 6.845-fold after phoxim and high temperature (30 °C) exposure, respectively, indicating that BmC1-THF synthase gene may play a significant role in response of silkworm to oxidative stresses.

Authors+Show Affiliations

School of Basic Medicine and Biological Sciences, Soochow University, Suzhou, Jiangsu 215123, PR China.School of Basic Medicine and Biological Sciences, Soochow University, Suzhou, Jiangsu 215123, PR China.School of Basic Medicine and Biological Sciences, Soochow University, Suzhou, Jiangsu 215123, PR China.School of Basic Medicine and Biological Sciences, Soochow University, Suzhou, Jiangsu 215123, PR China.School of Basic Medicine and Biological Sciences, Soochow University, Suzhou, Jiangsu 215123, PR China.School of Basic Medicine and Biological Sciences, Soochow University, Suzhou, Jiangsu 215123, PR China.School of Basic Medicine and Biological Sciences, Soochow University, Suzhou, Jiangsu 215123, PR China.School of Basic Medicine and Biological Sciences, Soochow University, Suzhou, Jiangsu 215123, PR China; National Engineering Laboratory for Modern Silk, Soochow University, Suzhou, Jiangsu 215123, PR China.School of Basic Medicine and Biological Sciences, Soochow University, Suzhou, Jiangsu 215123, PR China; National Engineering Laboratory for Modern Silk, Soochow University, Suzhou, Jiangsu 215123, PR China. Electronic address: lib@suda.edu.cn.

Pub Type(s)

Journal Article

Language

eng

PubMed ID

29660516

Citation

Chen, Meijun, et al. "Molecular Cloning and Characterization of C1 Tetrahydrofolate (C1-THF) Synthase in Bombyx Mori, Silkworm." Gene, vol. 663, 2018, pp. 25-33.
Chen M, Zhai J, Liu Y, et al. Molecular cloning and characterization of C1 tetrahydrofolate (C1-THF) synthase in Bombyx mori, silkworm. Gene. 2018;663:25-33.
Chen, M., Zhai, J., Liu, Y., Xue, B., Hu, J., Cheng, X., Li, J., Hu, J., & Li, B. (2018). Molecular cloning and characterization of C1 tetrahydrofolate (C1-THF) synthase in Bombyx mori, silkworm. Gene, 663, 25-33. https://doi.org/10.1016/j.gene.2018.04.037
Chen M, et al. Molecular Cloning and Characterization of C1 Tetrahydrofolate (C1-THF) Synthase in Bombyx Mori, Silkworm. Gene. 2018 Jul 15;663:25-33. PubMed PMID: 29660516.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Molecular cloning and characterization of C1 tetrahydrofolate (C1-THF) synthase in Bombyx mori, silkworm. AU - Chen,Meijun, AU - Zhai,Jingjie, AU - Liu,Yu, AU - Xue,Bin, AU - Hu,Jiahuan, AU - Cheng,Xiaoyu, AU - Li,Jinxin, AU - Hu,Jingsheng, AU - Li,Bing, Y1 - 2018/04/14/ PY - 2017/12/29/received PY - 2018/04/11/revised PY - 2018/04/13/accepted PY - 2018/4/17/pubmed PY - 2018/5/31/medline PY - 2018/4/17/entrez KW - Folate metabolism KW - High temperature KW - Oxidative stress KW - Phoxim SP - 25 EP - 33 JF - Gene JO - Gene VL - 663 N2 - Folate metabolism pathway is mainly associated with syntheses of nucleic acids and proteins as well as DNA methylation and repair. Cytoplasmic C1 tetrahydrofolate (C1-THF) synthase is a central enzyme in folate metabolism and plays an important role in C1-THF conversion. The full-length sequence of silkworm (Bombyx mori) cytoplasmic C1-THF synthase (BmC1-THF synthase) gene including an open reading frame (ORF) of 932 amino acid residues was cloned. Phylogenetic analysis indicated that BmC1-THF synthase shares 84% and 81% identity with C1-THF synthase of Papilio Xuthus and Danaus plexippus, respectively. Conserved sequence analysis showed that the 330 to 710 amino acid residues of BmC1-THF synthase were highly conserved among various organisms. Recombinant BmC1-THF synthase protein with a molecular weight of about 105.5 kDa was expressed in E. coli cells and identified using SDS-PAGE and western blot analysis. The expression of BmC1-THF synthase gene in eight silkworm tissues revealed that BmC1-THF synthase gene is widely expressed in various tissues of silkworm and highly expressed in the fat body. The expression characteristics of BmC1-THF synthase gene in response to oxidative stress were conducted under phoxim and high temperature (30 °C) exposure. The results showed that the transcriptional level of BmC1-THF synthase gene was upregulated by 3.435-fold and 6.845-fold after phoxim and high temperature (30 °C) exposure, respectively, indicating that BmC1-THF synthase gene may play a significant role in response of silkworm to oxidative stresses. SN - 1879-0038 UR - https://www.unboundmedicine.com/medline/citation/29660516/Molecular_cloning_and_characterization_of_C1_tetrahydrofolate__C1_THF__synthase_in_Bombyx_mori_silkworm_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0378-1119(18)30405-0 DB - PRIME DP - Unbound Medicine ER -