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Glutamate production by Corynebacterium glutamicum: dependence on the oxoglutarate dehydrogenase inhibitor protein OdhI and protein kinase PknG

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Abstract

We recently showed that the activity of the 2-oxoglutarate dehydrogenase complex (ODHC) in Corynebacterium glutamicum is controlled by a novel regulatory mechanism that involves a 15-kDa protein called OdhI and serine/threonine protein kinase G (PknG). In its unphosphorylated state, OdhI binds to the E1 subunit (OdhA) of ODHC and, thereby, inhibits its activity. Inhibition is relieved by phosphorylation of OdhI at threonine-14 by PknG under conditions requiring high ODHC activity. In this work, evidence is provided that the dephosphorylation of phosphorylated OdhI is catalyzed by a phospho-Ser/Thr protein phosphatase encoded by the gene cg0062, designated ppp. As a decreased ODHC activity is important for glutamate synthesis, we investigated the role of OdhI and PknG for glutamate production under biotin limitation and after addition of Tween-40, penicillin, or ethambutol. A ΔodhI mutant formed only 1–13% of the glutamate synthesized by the wild type. Thus, OdhI is essential for efficient glutamate production. The effect of a pknG deletion on glutamate synthesis was dependent on the induction conditions. Under strong biotin limitation and in the presence of ethambutol, the ΔpknG mutant showed significantly increased glutamate production, offering a new way to improve production strains.

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Abbreviations

cdw:

cell dry weight

PknG:

serine/threonine protein kinase G

ODHC:

2-oxoglutarate dehydrogenase complex

OdhI:

oxoglutarate dehydrogenase inhibitor protein

TCA cycle:

tricarboxylic acid cycle

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Correspondence to Michael Bott.

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Dedicated to Prof. Dr. Hermann Sahm on the occasion of his 65th birthday

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Schultz, C., Niebisch, A., Gebel, L. et al. Glutamate production by Corynebacterium glutamicum: dependence on the oxoglutarate dehydrogenase inhibitor protein OdhI and protein kinase PknG. Appl Microbiol Biotechnol 76, 691–700 (2007). https://doi.org/10.1007/s00253-007-0933-9

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  • DOI: https://doi.org/10.1007/s00253-007-0933-9

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