Cookies help us deliver our services. By using our services, you agree to our use of cookies. More information

Angerer 2011 Biochem J

From Bioblast
Publications in the MiPMap
Angerer H, Zwicker K, Wumaier Z, Sokolova L, Heide H, Steger M, Kaiser S, Nübel E, Brutschy B, Radermacher M, Brandt U, Zickermann V (2011) A scaffold of accessory subunits links the peripheral arm and the distal proton-pumping module of mitochondrial complex I. https://doi.org/10.1042/bj20110359

» Biochem J 437:279-88. PMID: 21545356 Open Access

Angerer Heike, Zwicker Klaus, Wumaier Zibiernisha, Sokolova Lucie, Heide Heinrich, Steger Micro, Kaiser Silke, Nuebel Esther, Brutschy Bernhard, Radermacher Michael, Brandt Ulrich, Zickermann Volker (2011) Biochem J

Abstract: Mitochondrial NADH:ubiquinone oxidoreductase (complex I) is a very large membrane protein complex with a central function in energy metabolism. Complex I from the aerobic yeast Yarrowia lipolytica comprises 14 central subunits that harbour the bioenergetic core functions and at least 28 accessory subunits. Despite progress in structure determination, the position of individual accessory subunits in the enzyme complex remains largely unknown. Proteomic analysis of subcomplex Iδ revealed that it lacked eleven subunits, including the central subunits ND1 and ND3 forming the interface between the peripheral and the membrane arm in bacterial complex I. This unexpected observation provided insight into the structural organization of the connection between the two major parts of mitochondrial complex I. Combining recent structural information, biochemical evidence on the assignment of individual subunits to the subdomains of complex I and sequence-based predictions for the targeting of subunits to different mitochondrial compartments, we derived a model for the arrangement of the subunits in the membrane arm of mitochondrial complex I.

Bioblast editor: Plangger M


Labels: MiParea: mt-Structure;fission;fusion 



Enzyme: Complex I