Proteomics

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Acetylome and succinylome of Corynebacterium glutamicum

ABSTRACT: Profiles of two major acyl-modifications, lysine acetylation and succinylation, under L-glutamate-producting and non-producing conditions in Corynebacterium glutamicum, which is industrially utilized for amino acid fermentation, was analyzed. During glutamate overproduction induced by Tween 40, global lysine acetylation was decreased, while lysine succinylation was increased. A label-free semi-quantitative proteomic analysis identified 591 acetylated proteins with 1,509 unique acetylation sites and 297 succinylated proteins with 790 unique succinylation sites. Lysine acetylation and succinylation targeted most enzymes in the central carbon metabolic pathways that are directly related to glutamate production, including the 2-oxoglutarate dehydrogenase complex (ODHC), a key enzyme for glutamate overproduction.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Corynebacterium Glutamicum (strain Atcc 13032 / K051)

TISSUE(S): Cell Lysate

SUBMITTER: Saori Kosono  

LAB HEAD: Saori Kosono

PROVIDER: PXD001662 | Pride | 2015-12-21

REPOSITORIES: Pride

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Publications

Altered acetylation and succinylation profiles in Corynebacterium glutamicum in response to conditions inducing glutamate overproduction.

Mizuno Yuta Y   Nagano-Shoji Megumi M   Kubo Shosei S   Kawamura Yumi Y   Yoshida Ayako A   Kawasaki Hisashi H   Nishiyama Makoto M   Yoshida Minoru M   Kosono Saori S  

MicrobiologyOpen 20151211 1

The bacterium Corynebacterium glutamicum is utilized during industrial fermentation to produce amino acids such as L-glutamate. During L-glutamate fermentation, C. glutamicum changes the flux of central carbon metabolism to favor L-glutamate production, but the molecular mechanisms that explain these flux changes remain largely unknown. Here, we found that the profiles of two major lysine acyl modifications were significantly altered upon glutamate overproduction in C. glutamicum; acetylation de  ...[more]

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