Dataset Information

Comprehensive Proteome Analyses of Lysine Acetylation in Tea leaves by sensing Nitrogen nutrition

ABSTRACT: Acetylation of lysine is a highly dynamic and reversibly regulated post-translational modification (PTM), which changes protein function in multiple ways [1]. As one of the most common PTMs to proteins in both eukaryotes and prokaryotes [1, 2], lysine acetylation occurred on either the α-amino group at the N-terminus of the protein or the ε-amino group on the side chain of lysine residues[3]. Since the first reveal of lysine acetylome in mammalian cells [4], acetylome in eukaryotes has been reported and the mechanistic studies indicated that lysine acetylation impacted various cellular processes including transcriptional regulation and metabolic stability [5-8]. In addition, a growing number of studies indicated that lysine acetylation widely existed in prokaryotes, and functional annotation showed lysine acetylation plays a crucial role in metabolic pathways, stress responses and enzymatic activity regulations in bacteria [9-11].

INSTRUMENT(S): Q Exactive

ORGANISM(S): Camellia Sinensis

TISSUE(S): Leaf

SUBMITTER: Rachel Green

LAB HEAD: Zhaotang Ding

PROVIDER: PXD008931 | Pride | 2018-11-30

REPOSITORIES: Pride

ACCESS DATA

Dataset's files

Source:

			Action	DRS
	6638TP-raw.zip	Other
	txt.zip	Other

Items per page:

1 - 2 of 2

Publications

Comprehensive proteome analyses of lysine acetylation in tea leaves by sensing nitrogen nutrition.

Jiang Jutang J Gai Zhongshuai Z Wang Yu Y Fan Kai K Sun Litao L Wang Hui H Ding Zhaotang Z

BMC genomics 20181126 1

<h4>Background</h4>N<sup>ε</sup>-Acetylation of lysine residues, a frequently occurring post-translational modification, plays important functions in regulating physiology and metabolism. However, the information of global overview of protein acetylome under nitrogen-starvation/resupply in tea (Camellia sinensis) leaves was limited. And the full function of lysine acetylated proteins of tea plants in nitrogen absorption and assimilation remains unclear.<h4>Results</h4>Here, we performed the glob ...[more]

PMID: 30477445

Similar Datasets

Project description:Background: Lysine crotonylation (Kcr), as a novel evolutionarily conserved type of PTM, is ubiquitous and essential in cell biology. However, its functions in tea plant, an important beverage crop, are largely unknown. Our study firstly attempted to describe Kcr proteins in tea leaves under NH4+ deficiency/resupply, and provided significant insights into exploring the physiological role of Kcr in plants for N utilization. Results: We performed the global analysis of crotonylome in tea plants under NH4+ deficiency/resupply using high-resolution LC-MS/MS coupled with highly sensitive immune-antibody. A total of 2288 kcr sites on 971 proteins were identified, of which contained in 15 types of Kcr motifs. Most of Kcr proteins were located in chloroplast and cytoplasm. 120 and 151 Kcr proteins were significantly changed at 3 hours and 3days of NH4+ resupply, respectively. Bioinformatics analysis showed that differentially expressed Kcr proteins participated in diverse biological processes such as photosynthesis, carbon fixation and amino acid metabolism, suggesting Kcr plays important roles in these processes. Interestingly, a large number of enzymes were crotonylated, and the activity and Kcr level of these enzymes changed significantly after NH4+ resupply, indicating a potential function of Kcr in the regulation of enzyme activities. Moreover, the protein-protein interaction analysis revealed that the diverse interactions of identified Kcr proteins mainly involved in photosynthesis, carbon fixation, amino acid metabolism and ribosome. Conclusions: The results suggested that lysine crotonylated proteins might play regulating roles in metabolic process in tea leaves under NH4+ deficiency/resupply. The critical regulatory roles mainly involved in diverse aspects of primary metabolic processes, especially in photosynthesis, carbon fixation and amino acid metabolism. The provided data may serve as important resources for exploring the physiological, biochemical, and genetic role of lysine crotonylation in tea plants.