Comprehensive Analysis of the Lysine Succinylome and Protein Co-modifications in Developing Rice Seeds.

ABSTRACT: Lysine succinylation has been recognized as a post-translational modification (PTM) in recent years. It is plausible that succinylation may have a vaster functional impact than acetylation because of bulkier structural changes and more significant charge differences on the modified lysine residue. Currently, however, the quantity and identity of succinylated proteins and their corresponding functions in cereal plants remain largely unknown. In this study, we estimated the native succinylation occupancy on lysine was between 2% to 10% in developing rice seeds. Eight hundred fifty-four lysine succinylation sites on 347 proteins have been identified by a thorough investigation in developing rice seeds. Six motifs were revealed as preferred amino acid sequence arrangements for succinylation si

SUBMITTER: Meng X 

PROVIDER: S-EPMC6885699 | biostudies-literature | 2019 Dec

REPOSITORIES: biostudies-literature