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J. Biol. Chem., Vol. 280, Issue 12, 11895-11901, March 25, 2005

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The Drosophila ninaG Oxidoreductase Acts in Visual Pigment Chromophore Production^*

Shanta Sarfare, Syed Tariq Ahmad, Michelle V. Joyce¶, Bill Boggess¶, and Joseph E. O'Tousa||

From the Departments of Biological Sciences and ^¶Chemistry and Biochemistry, University of Notre Dame, Notre Dame, Indiana 46556

The Drosophila ninaG mutant is characterized by low levels of Rh1 rhodopsin, because of the inability to transport this rhodopsin from the endoplasmic reticulum to the rhabdomere. ninaG mutants do not affect the biogenesis of the minor opsins Rh4 and Rh6. A genetic analysis placed the ninaG gene within the 86E4-86E6 chromosomal region. A sequence analysis of the 15 open reading frames within this region from the ninaG^P330 mutant allele identified a stop codon in the CG6728 gene. Germ-line transformation of the CG6728 genomic region rescued the ninaG mutant phenotypes, confirming that CG6728 corresponds to the ninaG gene. The NinaG protein belongs to the glucose-methanol-choline oxidoreductase family of flavin adenine dinucleotide-binding enzymes catalyzing hydroxylation and oxidation of a variety of small organic molecules. High performance liquid chromatography analysis of retinoids was used to gain insight into the in vivo role of the NinaG oxidoreductase. The results show that when Rh1 is expressed as the major rhodopsin, ninaG flies fail to accumulate 3-hydroxyretinal. Further, in transgenic flies expressing Rh4 as the major rhodopsin, 3-hydroxyretinal is the major retinoid in ninaG⁺, but a different retinoid profile is observed in ninaG^P330. These results indicate that the ninaG oxidoreductase acts in the biochemical pathway responsible for conversion of retinal to the rhodopsin chromophore, 3-hydroxyretinal.

Received for publication, October 28, 2004 , and in revised form, January 3, 2005.

^* This work was supported by Grant EY06808 from the National Institutes of Health. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Current address: Dept. of Vision Sciences, University of Alabama at Birmingham, Birmingham, AL 35294-4390.

^|| To whom correspondence should be addressed. Tel.: 574-631-6093; Fax: 574-631-7413; E-mail: jotousa{at}nd.edu.

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