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Molecular characterization and expression analysis of a phosphoserine aminotransferase involving l-serine synthesis from silkworm, Bombyx mori.
Arch Insect Biochem Physiol. 2019 Jun; 101(2):e21553.AI

Abstract

In this study, we identified and characterized a phosphoserine aminotransferase (bmPSAT) from Bombyx mori (B. mori) that is responsible for l-serine biosynthesis. A complementary DNA that encodes bmPSAT was cloned by reverse transcriptase polymerase reaction and sequenced. The presumed amino acid sequence revealed 47-87% identity with known PSATs from insects, humans, plants, and bacteria. Through phylogenetic analysis, we found that bmPSAT is evolutionary related to insect PSATs. Recombinant bmPSAT was produced in Escherichia coli by using a cold-shock promotor and purified to homogeneity. This enzyme utilizes phosphohydroxypyruvate and glutamate for transamination. bmPSAT messenger RNA (mRNA) was expressed at higher levels in several tissues of standard strain silkworm including the silk gland, whereas a sericin-deficient silkworm strain exhibited a diminished expression of bmPSAT mRNA in the silk gland. These findings indicate that bmPSAT may play an important role in synthesizing and supplying l-serine in the larva of B. mori.

Authors+Show Affiliations

Department of Bioscience and Biotechnology, Graduate School of Bioresource and Bioenvironmental Sciences, Faculty of Agriculture, Kyushu University, Fukuoka, Japan.Department of Bioscience and Biotechnology, Graduate School of Bioresource and Bioenvironmental Sciences, Faculty of Agriculture, Kyushu University, Fukuoka, Japan.Department of Bioscience and Biotechnology, Graduate School of Bioresource and Bioenvironmental Sciences, Faculty of Agriculture, Kyushu University, Fukuoka, Japan.Department of Bioscience and Biotechnology, Graduate School of Bioresource and Bioenvironmental Sciences, Faculty of Agriculture, Kyushu University, Fukuoka, Japan.Department of Bioscience and Biotechnology, Graduate School of Bioresource and Bioenvironmental Sciences, Faculty of Agriculture, Kyushu University, Fukuoka, Japan.Department of Bioscience and Biotechnology, Graduate School of Bioresource and Bioenvironmental Sciences, Faculty of Agriculture, Kyushu University, Fukuoka, Japan.Department of Bioscience and Biotechnology, Graduate School of Bioresource and Bioenvironmental Sciences, Faculty of Agriculture, Kyushu University, Fukuoka, Japan.Department of Bioscience and Biotechnology, Graduate School of Bioresource and Bioenvironmental Sciences, Faculty of Agriculture, Kyushu University, Fukuoka, Japan.

Pub Type(s)

Journal Article

Language

eng

PubMed ID

31004387

Citation

Haque, Mohammad R., et al. "Molecular Characterization and Expression Analysis of a Phosphoserine Aminotransferase Involving L-serine Synthesis From Silkworm, Bombyx Mori." Archives of Insect Biochemistry and Physiology, vol. 101, no. 2, 2019, pp. e21553.
Haque MR, Hirowatari A, Koyanagi A, et al. Molecular characterization and expression analysis of a phosphoserine aminotransferase involving l-serine synthesis from silkworm, Bombyx mori. Arch Insect Biochem Physiol. 2019;101(2):e21553.
Haque, M. R., Hirowatari, A., Koyanagi, A., Ichinose, T., Abiru, M., Mohri, S., Furuya, S., & Yamamoto, K. (2019). Molecular characterization and expression analysis of a phosphoserine aminotransferase involving l-serine synthesis from silkworm, Bombyx mori. Archives of Insect Biochemistry and Physiology, 101(2), e21553. https://doi.org/10.1002/arch.21553
Haque MR, et al. Molecular Characterization and Expression Analysis of a Phosphoserine Aminotransferase Involving L-serine Synthesis From Silkworm, Bombyx Mori. Arch Insect Biochem Physiol. 2019;101(2):e21553. PubMed PMID: 31004387.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Molecular characterization and expression analysis of a phosphoserine aminotransferase involving l-serine synthesis from silkworm, Bombyx mori. AU - Haque,Mohammad R, AU - Hirowatari,Aiko, AU - Koyanagi,Ayumi, AU - Ichinose,Takashi, AU - Abiru,Maiko, AU - Mohri,Shinya, AU - Furuya,Shigeki, AU - Yamamoto,Kohji, Y1 - 2019/04/19/ PY - 2019/02/01/received PY - 2019/03/12/revised PY - 2019/03/29/accepted PY - 2019/4/21/pubmed PY - 2019/5/30/medline PY - 2019/4/21/entrez KW - Bombyx mori KW - phosphoserine aminotransferase KW - serine KW - silkworm SP - e21553 EP - e21553 JF - Archives of insect biochemistry and physiology JO - Arch. Insect Biochem. Physiol. VL - 101 IS - 2 N2 - In this study, we identified and characterized a phosphoserine aminotransferase (bmPSAT) from Bombyx mori (B. mori) that is responsible for l-serine biosynthesis. A complementary DNA that encodes bmPSAT was cloned by reverse transcriptase polymerase reaction and sequenced. The presumed amino acid sequence revealed 47-87% identity with known PSATs from insects, humans, plants, and bacteria. Through phylogenetic analysis, we found that bmPSAT is evolutionary related to insect PSATs. Recombinant bmPSAT was produced in Escherichia coli by using a cold-shock promotor and purified to homogeneity. This enzyme utilizes phosphohydroxypyruvate and glutamate for transamination. bmPSAT messenger RNA (mRNA) was expressed at higher levels in several tissues of standard strain silkworm including the silk gland, whereas a sericin-deficient silkworm strain exhibited a diminished expression of bmPSAT mRNA in the silk gland. These findings indicate that bmPSAT may play an important role in synthesizing and supplying l-serine in the larva of B. mori. SN - 1520-6327 UR - https://www.unboundmedicine.com/medline/citation/31004387/Molecular_characterization_and_expression_analysis_of_a_phosphoserine_aminotransferase_involving_l_serine_synthesis_from_silkworm_Bombyx_mori_ L2 - https://doi.org/10.1002/arch.21553 DB - PRIME DP - Unbound Medicine ER -