Proteome-wide identification and functional analysis of ubiquitinated proteins in peach leaves.

ABSTRACT: Ubiquitination is a critical post-translational modification machinery that governs a wide range of cellular functions by regulating protein homeostasis. Identification of ubiquitinated proteins and lysine residues can help researchers better understand the physiological roles of ubiquitin modification in different biological systems. In this study, we report the first comprehensive analysis of the peach ubiquitome by liquid chromatography-tandem mass spectrometry-based diglycine remnant affinity proteomics. Our systematic profiling revealed a total of 544 ubiquitination sites on a total of 352 protein substrates. Protein annotation and functional analysis suggested that ubiquitination is involved in modulating a variety of essential cellular and physiological processes in peach, including

SUBMITTER: Song Y 

PROVIDER: S-EPMC7015887 | biostudies-literature | 2020 Feb

REPOSITORIES: biostudies-literature