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Raw mass spectrometry data for the identification of GmGNAT10 as a key acetyltransferase mediating acetylation modification of Rubisco in soybean

ABSTRACT: Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco), the core rate-limiting enzyme of photosynthetic carbon metabolism, is regulated by acetylation, yet its upstream acetyltransferases remain largely uncharacterized. Here, we identified a novel soybean acetyltransferase GmGNAT10, which interacts with Rubisco and other photosynthetic enzymes via IP-MS/MS interactomics. Quantitative acetylomics under fluctuating light revealed dramatic genotypic differences in acetylation levels of key RbcL lysine residues (K23, K175, K236) between wild-type and GmGNAT10 mutants. Our findings expand the mechanistic understanding of chloroplast non-histone acetylation in fine-tuning photosynthetic carbon metabolism.

ORGANISM(S): Glycine Max

SUBMITTER: Mingnan Qu

PROVIDER: PXD077705 | iProX | Tue Apr 28 00:00:00 BST 2026

REPOSITORIES: iProX

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