Juvenile Hormone Biosynthesis Gene Expression in the corpora allata of Honey Bee (Apis mellifera L.) Female Castes

One of the first tasks of worker honey bees (Apis mellifera) during their lifetime is to feed the larval offspring. In brief, young workers (nurse bees) secrete a special food jelly that contains a large amount of unique major royal jelly proteins (MRJPs). The regulation of mrjp gene expression is not well understood, but the large upregulation in well-fed nurse bees suggests a tight repression until, or a massive induction upon, hatching of the adult worker bees. The lipoprotein vitellogenin, the synthesis of which is regulated by the two systemic hormones 20-hydroxyecdysone and juvenile hormone, is thought to be a precursor for the production of MRJPs. Thus, the regulation of mrjp expression by the said systemic hormones is likely. This study focusses on the role of 20-hydroxyecdysone by elucidating its effect on mrjp gene expression dynamics. Specifically, we tested whether 20-hydroxyecdysone displayed differential effects on various mrjps. We found that the expression of the mrjps (mrjp1–3) that were finally secreted in large amounts into the food jelly, in particular, were down regulated by 20-hydroxyecdysone treatment, with mrjp3 showing the highest repression value.

Download Full-text

On the Specificity of Juvenile Hormone Biosynthesis in the Male Cecropia Moth

Zeitschrift für Naturforschung C ◽

10.1515/znc-1981-7-812 ◽

1981 ◽

Vol 36 (7-8) ◽

pp. 579-585 ◽

Cited By ~ 42

Author(s):

Martin G. Peter ◽

Paul D. Shirk ◽

Karl H. Dahm ◽

Herbert Roller

Keyword(s):

Juvenile Hormone ◽

Enzyme System ◽

Reaction Rates ◽

Corpora Allata ◽

Low Molecular Weight ◽

Methyltransferase Activity ◽

Accessory Sex Glands ◽

Juvenile Hormone Biosynthesis ◽

Hormone Biosynthesis ◽

Natural Enantiomer

Abstract The accessory sex glands (ASG) of adult male Cecropia contain an enzyme that methylates juvenile hormone acids (JH-acids) in the presence of S-adenosyl-L-methionine (SAM). The methyltransferase is highly specific. The reaction rates decrease in the order JH-I-acid, JH-II-acid and JH-III-acid; in each case the natural enantiomer is esterified predominantly. Methyltrans ferase activity with the same substrate specificity was also demonstrated in adult female corpora allata (CA). Male CA have only marginal methyltransferase activity. The CA of male H. cecropia contain substantial amounts of JH-I-acid and JH-II-acid (minimum: 5 pmol/pair). When kept in organ culture, they release JH-acids into the medium. Radiolabeled propionate and mevalonate are incorporated efficiently into the carbon skeletons of the JH-acids. The enzyme system performing these transformations cannot be forced to produce JH-III-acid even in the presence of high mevalonate concentrations, though homomevalonate may enhance biosynthesis of JH-I-acid and JH-II-acid more than tenfold. It becomes evident that the regulation of JH titer balances with regard to the homologous structures during insect development is not merely a question of the availability of low molecular weight precursors, but in addition that of highly specific enzymes acting as regulatory entities in the later steps of the biosynthetic sequence.

Download Full-text