Establishment of a landscape of UPL5-ubiquitinated on multiple subcellular components of leaf senescence cell in Arabidopsis

ABSTRACT: Catabolism of macromolecules is a major event in senescent cells, especially involving proteolysis of organelles and abnormally aggregated proteins, the circulation of nutrients, and precise control of intracellular environmental balance. Proteasomes are distributed in the nucleus and cytoplasm; however, proteasome in organelles is limited. In this study, multi-omics proteomic analyses of ubiquitinated proteins enriched by using antibody against “di-Gly-Lys” via a free labeling was used to investigate the global changes of protein levels and ubiquitination modification levels of upl5 mutant relative to wildtype plant; subcellular localization analysis of UPL5 was found to be located in the nucleus, cytoplasm and plastid within the cell; and the direct lysine site pattern of UPL5 were screened by the H89R substitution in the tagged ubiquitinated assay. It suggests that UPL5 acting as a candidate of organelle E3 ligase either in the nucleus or cytoplasm or plastid, modifies numerous targets related to nuclear transcription and plastid photosynthesis involving in Ca2+ and hormone signaling pathway in plant senescence and in response to (a)biotic stress protection.

ORGANISM(S): Arabidopsis Thaliana

SUBMITTER: Ying Miao  

PROVIDER: PXD033568 | iProX | Sat Apr 30 00:00:00 BST 2022

REPOSITORIES: iProX