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Papers In Press, published online ahead of print May 1, 2006
Medicine, University of Chicago, Chicago, IL 60637
Corresponding Author: hgrasber{at}uchicago.edu
Dual oxidase 2 (DUOX2), an NADPH:O2 oxidoreductase flavoprotein, is a component of the thyroid H2O2 generator crucial for hormone synthesis at the apical membrane. Mutations in DUOX2 produce congenital hypothyroidism in humans. However, no functional DUOX-based NADPH oxidase has ever been reconstituted at the plasma membrane of transfected cells. It has been proposed that DUOX retention in the endoplasmatic reticulum (ER) of heterologous systems is due to the lack of an unidentified component required for functional maturation of the enzyme. By data mining of a massively parallel signature sequencing tissue expression database, we identified an uncharacterized gene (named DUOX activator 2, DUOXA2) arranged head-to-head to and co-expressed with DUOX2. A paralog (DUOXA1) was similarly linked to DUOX1. The genomic rearrangement leading to linkage of ancient DUOX and DUOXA genes could be traced back before the divergence of echinoderms. We demonstrate that co-expression of DUOXA2, an ER-resident transmembrane protein, allows ER-to-Golgi transition, maturation, and translocation to the plasma membrane of functional DUOX2 in a heterologous system. The identification of DUOXA genes has important implications for studies of the molecular mechanisms controlling DUOX expression and the molecular genetics of congenital hypothyroidism.
J. Biol. Chem, 10.1074/jbc.C600095200
Submitted on April 24, 2006
Accepted on May 1, 2006
Identification of the maturation factor for dual oxidase: Evolution of an eukaryotic operon equivalent
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