{"database":"iProX","file_versions":[],"scores":null,"additional":{"omics_type":["Proteomics"],"submitter":["Mingnan Qu"],"species":["Glycine Max"],"full_dataset_link":["http://www.iprox.org/page/project.html?id=IPX0016878000"],"submitter_email":["qmn@yzu.edu.cn"],"submitter_affiliation":["College of Agriculture"],"sample_protocol":[""],"repository":["iProX"],"data_protocol":[""],"additional_accession":[]},"is_claimable":false,"name":"Raw mass spectrometry data for the identification of GmGNAT10 as a key acetyltransferase mediating acetylation modification of Rubisco in soybean","description":"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.","dates":{"publication":"Tue Apr 28 00:00:00 GMT+01:00 2026"},"accession":"PXD077705","cross_references":{"TAXONOMY":["3847"]}}