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The novel component Kgd4 recruits the E3 subunit to the mitochondrial alpha-ketoglutarate dehydrogenase
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
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2014 (English)In: Molecular Biology of the Cell, ISSN 1059-1524, E-ISSN 1939-4586, Vol. 25, no 21, 3342-3349 p.Article in journal (Refereed) Published
Abstract [en]

The mitochondrial citric acid cycle is a central hub of cellular metabolism, providing intermediates for biosynthetic pathways and channeling electrons to the respiratory chain complexes. In this study, we elucidated the composition and organization of the multienzyme complex alpha-ketoglutarate dehydrogenase (alpha-KGDH). In addition to the three classical E1-E3 subunits, we identified a novel component, Kgd4 (Ymr31/MRPS36), which was previously assigned to be a subunit of the mitochondrial ribosome. Biochemical analyses demonstrate that this protein plays an evolutionarily conserved role in the organization of mitochondrial alpha-KGDH complexes of fungi and animals. By binding to both the E1-E2 core and the E3 subunit, Kgd4 acts as a molecular adaptor that is necessary to a form a stable alpha-KGDH enzyme complex. Our work thus reveals a novel subunit of a key citric acid-cycle enzyme and shows how this large complex is organized.

Place, publisher, year, edition, pages
2014. Vol. 25, no 21, 3342-3349 p.
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Biological Sciences
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URN: urn:nbn:se:su:diva-110181DOI: 10.1091/mbc.E14-07-1178ISI: 000344236100017OAI: oai:DiVA.org:su-110181DiVA: diva2:787509
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AuthorCount:7;

Available from: 2015-02-10 Created: 2014-12-08 Last updated: 2017-12-04Bibliographically approved

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Heublein, ManfredTeixeira, Pedro F.Ott, Martin
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