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J Biol Chem, Vol. 275, Issue 18, 13986-13993, May 5, 2000

Processing and Maturation of Flavocytochrome b558 Include Incorporation of Heme as a Prerequisite for Heterodimer Assembly*

Frank R. DeLeoDagger §, James B. Burritt||, Lixin Yu**, Algirdas J. Jesaitis, Mary C. Dinauer**, and William M. NauseefDagger Dagger Dagger

From the Dagger  Inflammation Program and the Department of Medicine, Veterans Affairs Medical Center and University of Iowa, Iowa City, Iowa 52242, the ** Wells Center for Pediatric Research, Riley Hospital for Children, Indiana University School of Medicine, Indianapolis, Indiana 46202, and the  Department of Microbiology, Montana State University, Bozeman, Montana 59715

The phagocyte NADPH-dependent oxidase generates superoxide by reducing molecular oxygen through a transmembrane heterodimer known as flavocytochrome b558 (flavocytochrome b). We investigated the biosynthesis of flavocytochrome b subunits gp91phox and p22phox to elucidate features of flavocytochrome b processing in myeloid cells. Although the gp91phox precursor, gp65, was processed to gp91phox within 4-8 h of chase, unassembled gp65 and p22phox monomers were degraded by the cytosolic proteasome. gp65 associated with p22phox post-translationally, within 1-4 h of chase, but prior to its modification in the Golgi complex. Moreover, p22phox coprecipitated with unglycosylated gp91phox primary translation product made in the presence of tunicamycin, suggesting that heterodimer formation does not require glycosylation. Blocking heme synthesis with succinyl acetone completely inhibited heterodimer formation, although biogenesis of gp65 and p22phox was unaffected. In succinyl acetone-treated cells, p22phox and gp65 were degraded completely by 8 h of chase, a process mediated by the cytosolic proteasome. Taken together, these data suggest that the formation of the gp65-p22phox heterodimer is relatively inefficient and that acquisition of heme by gp65 precedes and is required for its association with p22phox, a process that requires neither the addition of N-linked oligosaccharides nor modification in the Golgi complex.

* This work was supported in part by Training Grant AI 07260-09 (to F. R. D.), Grants RO1 AI 34879 and HL 53592 (to W. M. N.), Grants PO1 HL 353586 and RO1 HL 45635 (to M. C. D.), and Grant RO1 AI 26711 (to A. J. J.) from the United States Public Health Service and by a Veterans Affairs Medical Center Merit Review (to W. M. N.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ Performed this work during the tenure of Post-doctoral Fellowship 9920491Z from the American Heart Association.

|| Performed this work during the tenure of Post-doctoral Fellowship 9704584S from the American Heart Association.

Dagger Dagger To whom correspondence should be addressed: Dept. of Medicine, University of Iowa, 200 Hawkins Dr., Iowa City, IA 52246. Tel.: 319-356-1739; Fax: 319-356-4600; E-mail: william-nauseef@uiowa.edu.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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