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Isolation and characterization of the trehalose‐6‐phosphate synthase gene from Locusta migratoria manilensis
Author(s) -
Cui ShuYan,
Xia YuXian
Publication year - 2009
Publication title -
insect science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.991
H-Index - 45
eISSN - 1744-7917
pISSN - 1672-9609
DOI - 10.1111/j.1744-7917.2009.01268.x
Subject(s) - trehalose , biology , complementary dna , hemolymph , biochemistry , migratory locust , gene , open reading frame , atp synthase , amino acid , microbiology and biotechnology , peptide sequence , locust , botany
Trehalose plays an important role in protecting organisms from various stresses. Trehalose‐6‐phosphate synthase (TPS) is the key enzyme in trehalose synthesis, but in insects only a few TPS genes have been identified and their function has not been well characterized. To better understand the function of TPS in insects, a complete TPS complementary DNA (cDNA) clone was obtained from the fat body of the locust Locusta migratoria manilensis (GenBank accession number: EU131894). The full‐length cDNA is 2 806 bp, including an open reading frame of 2 442 bp, which encodes an 813 amino acids protein with a calculated molecular weight of 91 976 Daltons and an isoelectric point of 6.14. The deduced amino acid sequence is highly similar to other published insect TPS and its C‐terminal also has a region homologous to trehalose phosphate phsophatase (TPP). Semi‐quantitative analysis indicated that the TPS transcript was expressed not only in fat body, but also in gut, hemolymph and leg muscle. These data may facilitate studies of TPS function in insects and improve our understanding of trehalose metabolism.