Isolation of juvenile hormone esterase and its partial cDNA clone from the beetle, Tenebrio molitor

• Published in: Insect biochemistry and molecular biology Vol. 30; no. 7; pp. 529 - 540
• Main Authors: Thomas, Beth Ann, Hinton, Andrew C, Moskowitz, Haim, Severson, Tonya F, Hammock, Bruce D
• Format: Journal Article
• Language: English
• Published: England Elsevier Ltd 01.07.2000
• Subjects: Affinity chromatography; Animals; Carboxylic Ester Hydrolases - chemistry; Carboxylic Ester Hydrolases - genetics; Carboxylic Ester Hydrolases - isolation & purification; Cloning, Molecular; DNA, Complementary - genetics; DNA, Complementary - isolation & purification; Electrophoresis, Polyacrylamide Gel; Esterase; Heliothis virescens; Hormones; Insects; Juvenile hormone esterase; Juvenile hormones; Juvenile Hormones - metabolism; Ligands; Sequence Analysis, Protein; Tenebrio - enzymology; Tenebrio - genetics; Tenebrio molitor; Hormones; Esterase; Insects; Tenebrio molitor; Affinity chromatography; Juvenile hormones
• ISSN: 0965-1748; 1879-0240
• DOI: 10.1016/S0965-1748(00)00020-5

Juvenile hormone esterase (JHE) plays an essential role in insect development. It is partially responsible for the clearance of juvenile hormone (JH) which regulates various aspects of insect development and reproduction. Because of its role in regulating JH titer, this enzyme has been targeted for development of biologically-based insecticides. JHE was partially purified from the beetle, Tenebrio molitor, using a transition state analog as the affinity ligand. Two forms of JHE were characterized by activity analysis, isoelectric focusing, two-dimensional SDS–PAGE and N-terminal sequence analysis. The esterase is associated with two proteins of sizes 71 and 150 kDa, both of which are active on JH III. A partial cDNA clone for the enzyme was isolated based on the sequence of N-terminal and internal peptides. Its sequence indicates that JHE from T. molitor and Heliothis virescens may have a common origin.