Mitochondrial protein import: precursor oxidation in a ternary complex with disulfide carrier and sulfhydryl oxidase
Identifieur interne : 000F82 ( Pmc/Curation ); précédent : 000F81; suivant : 000F83Mitochondrial protein import: precursor oxidation in a ternary complex with disulfide carrier and sulfhydryl oxidase
Auteurs : Diana Stojanovski ; Dusanka Milenkovic ; Judith M. Müller ; Kipros Gabriel ; Agnes Schulze-Specking ; Michael J. Baker [Australie] ; Michael T. Ryan [Australie] ; Bernard Guiard [France] ; Nikolaus Pfanner [Allemagne] ; Agnieszka Chacinska [Allemagne]Source :
- The Journal of Cell Biology [ 0021-9525 ] ; 2008.
Abstract
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.
Url:
DOI: 10.1083/jcb.200804095
PubMed: 18852299
PubMed Central: 2568017
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Diana Stojanovski<affiliation><nlm:aff wicri:cut=", and" id="N0x3a3fdd0N0x400fa70">Institut für Biochemie und Molekularbiologie, Zentrum für Biochemie und Molekulare Zellforschung</nlm:aff>
<wicri:noCountry code="subfield">Zentrum für Biochemie und Molekulare Zellforschung</wicri:noCountry>
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<affiliation><nlm:aff wicri:cut=", and" id="N0x3a3fdd0N0x400fa70">Institut für Biochemie und Molekularbiologie, Zentrum für Biochemie und Molekulare Zellforschung</nlm:aff>
<wicri:noCountry code="subfield">Zentrum für Biochemie und Molekulare Zellforschung</wicri:noCountry>
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<affiliation><nlm:aff wicri:cut=", and" id="N0x3a3fdd0N0x400fa70">Institut für Biochemie und Molekularbiologie, Zentrum für Biochemie und Molekulare Zellforschung</nlm:aff>
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<front><div type="abstract" xml:lang="en"><p>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.</p>
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<title-group><article-title>Mitochondrial protein import: precursor oxidation in a ternary complex with disulfide carrier and sulfhydryl oxidase</article-title>
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<contrib-group><contrib contrib-type="author"><name><surname>Stojanovski</surname>
<given-names>Diana</given-names>
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<contrib contrib-type="author"><name><surname>Pfanner</surname>
<given-names>Nikolaus</given-names>
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<xref ref-type="aff" rid="N0x3a3fdd0N0x400fa70">1</xref>
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<contrib contrib-type="author"><name><surname>Chacinska</surname>
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Institut für Biochemie und Molekularbiologie, Zentrum für Biochemie und Molekulare Zellforschung, and<label>2</label>
Centre for Biological Signalling Studies (<italic>bioss</italic>
), Universität Freiburg, 79104 Freiburg, Germany</aff>
<aff id="aff3"><label>3</label>
Department of Biochemistry, La Trobe University, Melbourne 3086, Australia</aff>
<aff id="aff4"><label>4</label>
Centre de Génétique Moléculaire, Centre National de la Recherche Scientifique, 91190 Gif-sur-Yvette, France</aff>
<author-notes><fn><p>Correspondence to Nikolaus Pfanner: <email>nikolaus.pfanner@biochemie.uni-freiburg.de</email>
; or Agnieszka Chacinska: <email>agnieszka.chacinska@biochemie.uni-freiburg.de</email>
</p>
</fn>
</author-notes>
<pub-date pub-type="ppub"><day>20</day>
<month>10</month>
<year>2008</year>
</pub-date>
<volume>183</volume>
<issue>2</issue>
<fpage>195</fpage>
<lpage>202</lpage>
<history><date date-type="received"><day>17</day>
<month>4</month>
<year>2008</year>
</date>
<date date-type="accepted"><day>15</day>
<month>9</month>
<year>2008</year>
</date>
</history>
<permissions><copyright-statement>© 2008 Stojanovski et al.</copyright-statement>
<license><p>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 <ext-link ext-link-type="uri" xlink:href="http://www.jcb.org/misc/terms.shtml">http://www.jcb.org/misc/terms.shtml</ext-link>
). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at <ext-link ext-link-type="uri" xlink:href="http://creativecommons.org/licenses/by-nc-sa/3.0/">http://creativecommons.org/licenses/by-nc-sa/3.0/</ext-link>
).</p>
</license>
</permissions>
<self-uri xlink:title="pdf" xlink:href="jcb1830195.pdf"></self-uri>
<abstract><p>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.</p>
</abstract>
</article-meta>
<notes><fn-group><fn><p>D. Stojanovski and D. Milenkovic contributed equally to this paper.</p>
</fn>
<fn><p>K. Gabriel's present address is Department of Genetics, University of Melbourne, Parkville 3010, Australia</p>
</fn>
<fn><p>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.</p>
</fn>
</fn-group>
</notes>
</front>
</pmc>
</record>
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