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.
| Original language | English |
|---|---|
| Article number | e21553 |
| Journal | Archives of insect biochemistry and physiology |
| Volume | 101 |
| Issue number | 2 |
| DOIs | |
| Publication status | Published - Jun 2019 |
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All Science Journal Classification (ASJC) codes
- Physiology
- Biochemistry
- Insect Science
Cite this
Molecular characterization and expression analysis of a phosphoserine aminotransferase involving l-serine synthesis from silkworm, Bombyx mori. / Haque, Mohammad R.; Hirowatari, Aiko; Koyanagi, Ayumi; Ichinose, Takashi; Abiru, Maiko; Mohri, Shinya; Furuya, Shigeki; Yamamoto, Kohji.
In: Archives of insect biochemistry and physiology, Vol. 101, No. 2, e21553, 06.2019.Research output: Contribution to journal › Article
}
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
PY - 2019/6
Y1 - 2019/6
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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=85065718182&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=85065718182&partnerID=8YFLogxK
U2 - 10.1002/arch.21553
DO - 10.1002/arch.21553
M3 - Article
C2 - 31004387
AN - SCOPUS:85065718182
VL - 101
JO - Archives of Insect Biochemistry and Physiology
JF - Archives of Insect Biochemistry and Physiology
SN - 0739-4462
IS - 2
M1 - e21553
ER -