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Updated: Jun 22, 2026
Dissection and Immunohistochemistry of Larval, Pupal and Adult Drosophila Retinas
Published on: November 14, 2012
Identification and characterization of retinoid-active short-chain dehydrogenases/reductases in Drosophila
Olga V Belyaeva1, Seung-Ah Lee, Oleg V Kolupaev
1Division of Biochemistry and Molecular Genetics, School of Medicine, University of Alabama-Birmingham, 720 20th Street South, 466 Kaul Genetics Building, Birmingham, AL 35294, USA. belyaeva@uab.edu
Background:
In chordates, retinoid metabolism is an important target of short-chain dehydrogenases/reductases (SDRs). It is not known whether SDRs play a role in retinoid metabolism of protostomes, such as Drosophila melanogaster.
Methods:
Drosophila genome was searched for genes encoding proteins with approximately 50% identity to human retinol dehydrogenase 12 (RDH12). The corresponding proteins were expressed in Sf9 cells and biochemically characterized. Their phylogenetic relationships were analyzed using PHYLIP software.
Results:
A total of six Drosophila SDR genes were identified. Five of these genes are clustered on chromosome 2 and one is located on chromosome X. The deduced proteins are 300 to 406 amino acids long and are associated with microsomal membranes. They recognize all-trans-retinaldehyde and all-trans-3-hydroxyretinaldehyde as substrates and prefer NADPH as a cofactor. Phylogenetically, Drosophila SDRs belong to the same branch of the SDR superfamily as human RDH12, indicating a common ancestry early in bilaterian evolution, before a protostome-deuterostome split.
Conclusions:
Similarities in the substrate and cofactor specificities of Drosophila versus human SDRs suggest conservation of their function in retinoid metabolism throughout protostome and deuterostome phyla.
General Significance:
The discovery of Drosophila retinaldehyde reductases sheds new light on the conversion of beta-carotene and zeaxantine to visual pigment and provides a better understanding of the evolutionary roots of retinoid-active SDRs.
