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Mitochondrial protein import: precursor oxidation in a ternary complex with disulfide carrier and sulfhydryl oxidase
Correspondence to Nikolaus Pfanner: nikolaus.pfanner{at}biochemie.uni-freiburg.de; or Agnieszka Chacinska: agnieszka.chacinska{at}biochemie.uni-freiburg.de
The biogenesis of mitochondrial intermembrane space proteins depends on specific machinery that transfers disulfide bonds to precursor proteins. The machinery shares features with protein relays for disulfide bond formation in the bacterial periplasm and endoplasmic reticulum. A disulfide-generating enzyme/sulfhydryl oxidase oxidizes a disulfide carrier protein, which in turn transfers a disulfide to the substrate protein. Current views suggest that the disulfide carrier alternates between binding to the oxidase and the substrate. We have analyzed the cooperation of the disulfide relay components during import of precursors into mitochondria and identified a ternary complex of all three components. The ternary complex represents a transient and intermediate step in the oxidation of intermembrane space precursors, where the oxidase Erv1 promotes disulfide transfer to the precursor while both oxidase and precursor are associated with the disulfide carrier Mia40.
K. Gabriel's present address is Department of Genetics, University of Melbourne, Parkville 3010, Australia
Abbreviations used in this paper: AMS, 4-acetamido-4'-maleimidylstilbene-2,2'-disulfonic acid; Dsb, disulfide bond formation protein; IMS, intermembrane space; MIA, mitochondrial IMS import and assembly; Tim, translocase of the inner mitochondrial membrane.
© 2008 Stojanovski et al. This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.jcb.org/misc/terms.shtml). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/).
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