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National Academy of Sciences, Proceedings of the National Academy of Sciences, 3(98), p. 1130-1135, 2001

DOI: 10.1073/pnas.98.3.1130

National Academy of Sciences, Proceedings of the National Academy of Sciences, 3(98), p. 1130-1135

DOI: 10.1073/pnas.031576398

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Analysis of the blind Drosophila mutant ninaB identifies the gene encoding the key enzyme for vitamin A formation in vivo

Journal article published in 2001 by Armin Dreher, Cornelia Kiefer, Johannes von Lintig ORCID, Mathias F. Wernet, Klaus Vogt
This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

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Abstract

Visual pigments (rhodopsins) are composed of a chromophore (vitamin A derivative) bound to a protein moiety embedded in the retinal membranes. Animals cannot synthesize the visual chromophore de novo but rely on the uptake of carotenoids, from which vitamin A is formed enzymatically by oxidative cleavage. Despite its importance, the enzyme catalyzing the key step in vitamin A formation resisted molecular analyses until recently, when the successful cloning of a cDNA encoding an enzyme with beta,beta-carotene-15,15'-dioxygenase activity from Drosophila was reported. To prove its identity with the key enzyme for vitamin A formation in vivo, we analyzed the blind Drosophila mutant ninaB. In two independent ninaB alleles, we found mutations in the gene encoding the beta,beta-carotene-15,15'-dioxygenase. These mutations lead to a defect in vitamin A formation and are responsible for blindness of these flies.