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Molecular and Cellular Biology, December 2003, p. 8495-8504, Vol. 23, No. 23
0270-7306/03/$08.00+0     DOI: 10.1128/MCB.23.23.8495-8504.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

The Drosophila Selenoprotein BthD Is Required for Survival and Has a Role in Salivary Gland Development

So Yeon Kwon,1,2 Paul Badenhorst,3 F. Javier Martin-Romero,1,{dagger} Bradley A. Carlson,1 Bruce M. Paterson,4 Vadim N. Gladyshev,5 Byeong Jae Lee,2* and Dolph L. Hatfield1*

Basic Research Laboratory,1 Laboratory of Molecular Cell Biology,3 Laboratory of Biochemistry, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20892,4 Department of Biochemistry, University of Nebraska, Lincoln, Nebraska 68588,5 Laboratory of Molecular Genetics, School of Biological Sciences, Seoul National University, Seoul 151-742, Korea2

Received 31 March 2003/ Returned for modification 9 May 2003/ Accepted 21 August 2003

Selenium is implicated in many diseases, including cancer, but its function at the molecular level is poorly understood. BthD is one of three selenoproteins recently identified in Drosophila. To elucidate the function of BthD and the role of selenoproteins in cellular metabolism and health, we analyzed the developmental expression profile of this protein and used inducible RNA interference (RNAi) to ablate function. We find that BthD is dynamically expressed during Drosophila development. bthD mRNA and protein are abundant in the ovaries of female flies and are deposited into the developing oocyte. Maternally contributed protein and RNA persist during early embryonic development but decay by the onset of gastrulation. At later stages of embryogenesis, BthD is expressed highly in the developing salivary gland. We generated transgenic fly lines carrying an inducible gene-silencing construct, in which an inverted bthD genomic-cDNA hybrid is under the control of the Drosophila Gal4 upstream activation sequence system. Duplex RNAi induced from this construct targeted BthD mRNA for destruction and reduced BthD protein levels. We found that loss of BthD compromised salivary gland morphogenesis and reduced animal viability.

* Corresponding author. Mailing address for B. J. Lee: Laboratory of Molecular Genetics, School of Biological Sciences, Seoul National University, Seoul 151-742, Korea. Phone: 82-2-880-6775. Fax: 82-2-872-9019. E-mail: imbglmg{at}plaza.snu.ac.kr.. Mailing address for D. L. Hatfield: National Cancer Institute, National Institutes of Health, Building 37, Room 2D09, Bethesda, MD 20892. Phone: (301) 496-2797. Fax: (301) 435-4957. E-mail: hatfield{at}dc37a.nci.nih.gov.

{dagger} Present address: Departmento de Bioquimica y Biologia Molecular, Facultat de Ciencias, Universidad de Extremadura, 06071 Badajoz, Spain.

Molecular and Cellular Biology, December 2003, p. 8495-8504, Vol. 23, No. 23
0022-538X/03/$08.00+0     DOI: 10.1128/MCB.23.23.8495-8504.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



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