Dataset Information

Landscapes of post-translational modifications in Trypanosoma parasites

ABSTRACT: Proteins of all living cells undergo a myriad of posttranslational modifications (PTMs) that are critical to multifarious life processes. In this study, we describe the first comprehensive multiple PTM-omics atlas in parallel with quantitative proteome analyses of two representative species of trypanosomes, Trypanosoma brucei and T. evansi. Approximately 40,000 modified sites and 150 histone marks were identified in each species. Proteins involved in the redox system were mainly regulated in T. brucei, while proteins associated with motility were predominantly modified in T. evansi. The establishment of a database of multiple PTMs in the two parasites provides us with insight into the biological mechanisms that underpin life processes in trypanosomes with huge different life cycles.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Trypanosoma Brucei Brucei

SUBMITTER: Naiwen Zhang

LAB HEAD: Qijun Chen

PROVIDER: PXD016425 | Pride | 2020-06-30

REPOSITORIES: Pride

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Publications

Landscapes of Protein Posttranslational Modifications of African Trypanosoma Parasites.

Zhang Naiwen N Jiang Ning N Zhang Kai K Zheng Lili L Zhang Di D Sang Xiaoyu X Feng Ying Y Chen Ran R Yang Na N Wang Xinyi X Cheng Zhongyi Z Suo Xun X Lun Zhaorong Z Chen Qijun Q

iScience 20200418 5

Proteins of all living cells undergo a myriad of post-translational modifications (PTMs) that are critical to multifarious life processes. In this study, we describe the first comprehensive multiple PTM-omics atlas in parallel with quantitative proteome analyses of two representative species of African trypanosomes, Trypanosoma brucei and Trypanosoma evansi. Ten PTM types with approximately 40,000 modified sites and 150 histone marks with a fine map on each protein of the two African trypanosome ...[more]

PMID: 32403088

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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.

Dataset Information

Landscapes of post-translational modifications in Trypanosoma parasites

Publications

Landscapes of Protein Posttranslational Modifications of African Trypanosoma Parasites.

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