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Characterization and in vitro expression of arginine kinase gene in the invasive western flower thrips, Frankliniella occidentalis.
- Source :
-
Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology [Comp Biochem Physiol B Biochem Mol Biol] 2019 Mar; Vol. 229, pp. 51-57. Date of Electronic Publication: 2019 Jan 11. - Publication Year :
- 2019
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Abstract
- Arginine kinase (AK) plays a critical role in insect energy metabolism and has been proposed to be a potential insecticide target for commercial exploitation. In this study, the full length cDNA encoding a typical group 1 insect AK (FoAK) was isolated from the western flower thrips (WFT), Frankliniella occidentalis (Pergande). Sequence analysis showed that FoAK contains an open reading frame of 1068 nucleotides, which encods a protein of 355 amino acid residues including the signature sequence pattern of ATP-guanidino kinases. Genomic structure analysis showed that the coding region of FoAK contains five exons connected by four introns. RT-qPCR analysis revealed that the mRNA expression of FoAK was developmentally regulated with the lowest level in prepupal stage. Enzymatic activity analysis of the recombinant enzymes expressed in Escherichia coli showed that FoAK is highly stereo specific for L-arginine versus D-arginine and the apparent Michaelis constant for L-arginine (Km <superscript>Arg</superscript> ) is comparable to that of AKs from a variety of species. This research should enable further investigation of the function as well as in vitro screening for inhibitors of FoAK.<br /> (Copyright © 2019. Published by Elsevier Inc.)
- Subjects :
- Animals
Recombinant Proteins biosynthesis
Recombinant Proteins genetics
Arginine Kinase biosynthesis
Arginine Kinase chemistry
Arginine Kinase genetics
Gene Expression
Insect Proteins biosynthesis
Insect Proteins chemistry
Insect Proteins genetics
Introduced Species
Thysanoptera enzymology
Thysanoptera genetics
Subjects
Details
- Language :
- English
- ISSN :
- 1879-1107
- Volume :
- 229
- Database :
- MEDLINE
- Journal :
- Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology
- Publication Type :
- Academic Journal
- Accession number :
- 30641133
- Full Text :
- https://doi.org/10.1016/j.cbpb.2019.01.003