Structure and function of complex I in animals and plants – a comparative view
| Autor: | Hans-Peter Braun, Michael Senkler, Jennifer Senkler |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2017 |
| Předmět: |
0106 biological sciences
0301 basic medicine Models Molecular Physiology plant Plant Science Mitochondrion chemistry 01 natural sciences Cell membrane 03 medical and health sciences Dewey Decimal Classification::500 | Naturwissenschaften::580 | Pflanzen (Botanik) Genetics medicine reduced nicotinamide adenine dinucleotide dehydrogenase (ubiquinone) mitochondrion Animals animal NADH dehydrogenase complex comparative study chemistry.chemical_classification Electron Transport Complex I Molecular mass biology Kinase fungi Cell Membrane NADH dehydrogenase food and beverages Cell Biology General Medicine Plants Mitochondria 030104 developmental biology Enzyme medicine.anatomical_structure ddc:580 Biochemistry biology.protein molecular model metabolism 010606 plant biology & botany |
| Zdroj: | Physiologia Plantarum 161 (2017), Nr. 1 Physiologia Plantarum |
| Popis: | The mitochondrial NADH dehydrogenase complex (complex I) has a molecular mass of about 1000 kDa and includes 40–50 subunits in animals, fungi and plants. It is composed of a membrane arm and a peripheral arm and has a conserved L-like shape in all species investigated. However, in plants and possibly some protists it has a second peripheral domain which is attached to the membrane arm on its matrix exposed side at a central position. The extra domain includes proteins resembling prokaryotic gamma-type carbonic anhydrases. We here present a detailed comparison of complex I from mammals and flowering plants. Forty homologous subunits are present in complex I of both groups of species. In addition, five subunits are present in mammalian complex I, which are absent in plants, and eight to nine subunits are present in plant complex I which do not occur in mammals. Based on the atomic structure of mammalian complex I and biochemical insights into complex I architecture from plants we mapped the species-specific subunits. Interestingly, four of the five animal-specific and five of the eight to nine plant-specific subunits are localized at the inner surface of the membrane arm of complex I in close proximity. We propose that the inner surface of the membrane arm represents a workbench for attaching proteins to complex I, which are not directly related to respiratory electron transport, like nucleoside kinases, acyl-carrier proteins or carbonic anhydrases. We speculate that further enzyme activities might be bound to this micro-location in other groups of organisms. © 2017 Scandinavian Plant Physiology Society |
| Databáze: | OpenAIRE |
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