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| Hauptseite > Publikationsdatenbank > Cellular localization of the hybrid pyruvate/2-oxoglutarate dehydrogenase complex in the actinobacterium Corynebacterium glutamicum > print |
| Hauptseite > Publikationsdatenbank > Cellular localization of the hybrid pyruvate/2-oxoglutarate dehydrogenase complex in the actinobacterium Corynebacterium glutamicum > print |
| 001 | 1010606 | ||
| 005 | 20240207072432.0 | ||
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| 100 | 1 | _ | |0 P:(DE-Juel1)128943 |a Bott, Michael |b 0 |e Corresponding author |
| 245 | _ | _ | |a Cellular localization of the hybrid pyruvate/2-oxoglutarate dehydrogenase complex in the actinobacterium Corynebacterium glutamicum |
| 260 | _ | _ | |a Birmingham, Ala. |b ASM |c 2023 |
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| 520 | _ | _ | |a For many bacterial proteins, specific localizations within the cell have been demonstrated, but enzymes involved in central metabolism are usually considered to be homogenously distributed within the cytoplasm. Here, we provide an example for a spatially defined localization of a unique enzyme complex found in actinobacteria, the hybrid pyruvate/2-oxoglutarate dehydrogenase complex (PDH-ODH). In non-actinobacterial cells, PDH and ODH form separate multienzyme complexes of megadalton size composed of three different subunits, E1, E2, and E3. The actinobacterial PDH-ODH complex is composed of four subunits, AceE (E1p), AceF (E2p), Lpd (E3), and OdhA (E1oE2o). Using fluorescence microscopy, we observed that in Corynebacterium glutamicum, all four subunits are co-localized in distinct spots at the cell poles, and in larger cells, additional spots are present at mid-cell. These results further confirm the existence of the hybrid complex. The unphosporylated OdhI protein, which binds to OdhA and inhibits ODH activity, was co-localized with OdhA at the poles, whereas phosphorylated OdhI, which does not bind OdhA, was distributed in the entire cytoplasm. Isocitrate dehydrogenase and glutamate dehydrogenase, both metabolically linked to ODH, were evenly distributed in the cytoplasm. Based on the available structural data for individual PDH-ODH subunits, a novel supramolecular architecture of the hybrid complex differing from classical PDH and ODH complexes has to be postulated. Our results suggest that localization at the poles or at mid-cell is most likely caused by nucleoid exclusion and results in a spatially organized metabolism in actinobacteria, with consequences yet to be studied. |
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| 773 | _ | _ | |0 PERI:(DE-600)2807133-5 |a 10.1128/spectrum.02668-23 |n 5 |p 1-17 |t Microbiology spectrum |v 11 |x 2165-0497 |y 2023 |
| 856 | 4 | _ | |u https://juser.fz-juelich.de/record/1010606/files/APC600445597_Invoice-3.pdf |
| 856 | 4 | _ | |u https://juser.fz-juelich.de/record/1010606/files/neyrolles-et-al-2023-cellular-localization-of-the-hybrid-pyruvate-2-oxoglutarate-dehydrogenase-complex-in-the.pdf |y OpenAccess |
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