Free access
Issue
Apidologie
Volume 35, Number 1, January-February 2004
Page(s) 37 - 47
DOI http://dx.doi.org/10.1051/apido:2003068
Apidologie 35 (2004) 37-47
DOI: 10.1051/apido:2003068

A member of the short-chain dehydrogenase/reductase (SDR) superfamily is a target of the ecdysone response in honey bee (Apis mellifera) caste development

Karina R. Guiduglia, Christine Hepperleb and Klaus Hartfelderb, c

a  Departamento de Genética, FMRP - Universidade de São Paulo, 14040-900 Ribeirão Preto, Brazil
b  LS Entwicklungsphysiologie, Zoologisches Institut, Universität Tübingen, 72076 Tübingen, Germany $*$ Current address: Department of Molecular Biosciences, University of Adelaide, Adelaide SA 5005, Australia.
c  Departamento de Biologia, FFCLRP - Universidade de São Paulo, 14040-901 Ribeirão Preto, Brazil

(Received 3 April 2003; revised 11 June 2003; accepted 25 June 2003)

Abstract
Many aspects in caste polyphenism result from hormonally controlled differential gene expression. A DDRT-PCR screen for ecdysteroid-regulated genes in ovaries revealed a set of ESTs coding for metabolic enzymes. For a cDNA encoding a short-chain dehydrogenase/reductase (SDR) we obtained the complete coding sequence (246 amino acids), revealing the protein motifs typical of insect SDRs. Its initially high expression in early fifth-instar larvae vanished in prepupae. Expression levels in worker larvae were higher than in queen larvae, suggesting negative regulation by the caste-specific ecdysteroid titer. This finding was confirmed by in vitro exposure of competent worker ovaries to makisterone A. In contrast to whole body RNA extracts, two SDR transcripts were detected in the ovaries. Both had their expression downregulated by makisterone A. Hormonal regulation and tissue-specific expression pattern makes this SDR an interesting enzyme for comparative molecular studies on social insect caste polyphenisms.


Key words: Apis mellifera / differential display PCR / ecdysteroid / alcohol dehydrogenase / caste polyphenism

Correspondence and reprints: Klaus Hartfelder khartfel@rge.fmrp.usp.br

© INRA, EDP Sciences, DIB, AGIB 2004