Dataset Information

Salt stress downregulates 2-hydroxybutyrylation in Arabidopsis siliques

ABSTRACT: In this study, we compared the siliques from Arabidopsis thaliana under salt stress (Ss) with those in the control (Cs). The results showed that Khib was abundant in siliques. However, there were certain significant differences between the Ss and the Cs: Totally 3,810 normalized Khib sites on 1,254 proteins were identified in siliques under salt stress, and Khib was up-regulated at 96 sites on 78 proteins while down-regulated at 282 sites on 205 proteins in Ss silique. Among them, 13 proteins, including F4IVN6, Q9M1P5, and Q9LF33, had sites with the most significant regulation Khib modification. Bioinformatics analysis suggests that Khib mainly participates in glycolysis/gluconeogenesis and endocytosis. In particular, there were 117 Khib-modified proteins that were mapped to the protein interaction database, and the proteins with the most significant up-regulation of Khib sites were on P46422, O82514, Q38970, Q9LD57, and Q9STW6, while the most down-regulated sites were on Q9M9K1, Q9SF16, O24456, P83484, Q9FWA3, and P54609. In the KEGG pathway enrichment analysis, Khib-modified proteins were enriched in several pathways related to energy metabolism, including gluconeogenesis pathway, pentose phosphate pathway, and pyruvate metabolism.

INSTRUMENT(S): TMT quantitation analysis

ORGANISM(S): Arabidopsis Thaliana (mouse-ear Cress)

TISSUE(S): Silique

SUBMITTER: Geriqiqige Hong

LAB HEAD: Guojing Li

PROVIDER: PXD028116 | Pride | 2021-12-30

REPOSITORIES: Pride

ACCESS DATA

Publications

Salt stress downregulates 2-hydroxybutyrylation in Arabidopsis siliques.

Hong Geriqiqige G Su Xiaoyi X Xu Ke K Liu Bin B Wang Guangxia G Li Jing J Wang Ruigang R Zhu Mulan M Li Guojing G

Journal of proteomics 20210922

Lysine 2-hydroxyisobutyrylation (Khib) is one of the newly discovered post-translational modifications (PTMs) through protein acylation. It has been reported to be widely distributed in both eukaryotes and prokaryotes, and plays an important role in chromatin conformation change, gene transcription, protein subcellular localization, protein-protein interaction, signal transduction, and cellular proliferation. In this study, the Khib modification proteome of siliques from A. thaliana under salt s ...[more]

PMID: 34562664

Similar Datasets

Project description:N-glycosylation is an important posttranslational modification in all eukaryotes, but little is known about the N-glycoproteomes in microalgal systems. Here, N-glycoproteome of the model diatom Phaeodactylum tricornutum was unveiled. Totally, 893 different N-glycosylated sites from 649 proteins were identified from P. tricornutum. The new synthesized N-glycans were principally transferred to asparagine residues within the conserved N-X-S/T (where X is a residue other than proline) sequence of nascent polypeptide chains. Functional annotation of N-glycosylated proteins showed that 70% N-glycoproteins were involved in vesicular transport and posttranslational modification, protein turnover, chaperones, indicating the N-glycosylation was important for these functions. Of the all identified N-glycoproteins 45.3% were predicted to localize on chloroplast, which implied the widespread regulatory role of N-glycosylation in chloroplast. Furthermore, the enrichment results of N-glycoproteins indicated that compared to ‘Cellular component’ and ‘Biological process’ categories proteins related with the ‘Molecular function’ category were more prone to be N-glycosylated. And it was speculated that N-glycosylation played a vital regulatory role in catalytic activity of enzymes and metabolism processes of many small molecules. 47% of all enriched proteins were related with metabolic pathways. The functional annotation and enrichment of N-glycoproteins suggested that N-glycoproteins participated in a variety of important metabolic pathways and perform different functions in P. tricornutum. 12 proteins involved in the ER quality control mechanism and ER- associated degradation pathway were identified as N-glycosylated proteins, indicating that the N-glycosylated modification was important for their functions in the protein N-glycosylation pathway. Additionally, some interacted glycoproteins were classified from this study, which provided valuable information for studying the functions of these glycoproteins. In the study, the identification of N-glycosylation on nascent proteins expands our understanding of this PTM at a proteomics scale and may facilitate the elucidation of the precise function of proteins in this model diatom.

Dataset Information

Salt stress downregulates 2-hydroxybutyrylation in Arabidopsis siliques

Publications

Salt stress downregulates 2-hydroxybutyrylation in Arabidopsis siliques.

Similar Datasets

OmicsDI is part of the ELIXIR infrastructure