Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Analysis of Lysine Lactylation in CD4+ T cells of normal and EAU mouse

ABSTRACT: Primary CD4+ T cells were isolated from normal and EAU mice spleens and used for lactylome analysis.

INSTRUMENT(S): Bruker Daltonics timsTOF series

ORGANISM(S): Mus Musculus (mouse)

TISSUE(S): Spleen, T Cell

SUBMITTER: Shengping Hou

LAB HEAD: Shengping Hou

PROVIDER: PXD040514 | Pride | 2023-08-29

REPOSITORIES: Pride

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	EE369LPLaB1_Control_Slot1-52_1_21416.d.zip	Other
	EE369LPLaB1_EAU_Slot1-53_1_21418.d.zip	Other
	EE369LQB1_Control_Slot1-41_1_21398.d.zip	Other
	EE369LQB1_EAU_Slot1-42_1_21400.d.zip	Other
	Lactylome-Search.zip	Other

Items per page:

1 - 5 of 7

Similar Datasets

Analysis of lactylome refines key molecular reprogramming mechanisms during oil production in Nannochloropsis oceanica

Project description:Lysine lactylation as a type of posttranslational modifications (PTMs) is recently associated with chromatin remodeling and gene transcription, but lysine lactylation of histone and non-histone proteins has not yet been studied in Nannochloropsis oceanica. To examine the prevalence and function of lactylation in N. oceanica, protein lactylation modification profiles were tracked after nitrogen deprivation for three days using 4D label-free proteome method. Under nitrogen deprivation (ND) and nitrogen repletion (NR) cultivation conditions, we mapped lactylome of proliferating microalgal cells.

2024-07-03 | PXD038775 | Pride

Systematic Identification of the Lysine lactylation in the Protozoan Parasite Toxoplasma gondii

Project description:Lysine lactylation (Kla) is a new posttranslational modification (PTM) identified in histone and nonhistone proteins of several eukaryotic cells that directly activate gene expression and DNA replication. However, very little is known about their scope and cellular distribution in apicomplexan parasites that are important to public and animal health. Toxoplasma gondii, the agent of toxoplasmosis, is one of obligate intracellular apicomplexan parasite that can infect all kinds of nucleated cells of animals and humans. Using this parasite as model organism, herein, we produced the first global lysine lactylome profile through LC-MS/MS. Overall, a total of 983 Kla sites occurred on 523 lactylated proteins were identified in Toxoplasma tachyzoites, the acute toxoplasmosis-causing stage. Bioinformatics analysis revealed that these lactylated proteins are evolutionarily conserved and involved in a wide variety of cellular functions such as energy metabolism, gene regulation and protein biosynthesis. Moreover, the results from subcellular localization analysis and IFA showed that the majority of lactylated T. gondii proteins localized in the nucleus, indicating a potential impact of Kla on gene regulation. Notably, an extensive batch of parasite-specific proteins unique to Apicomplexa is lactylated in T. gondii. Our findings revealed that Kla was widespread in the early branching eukaryotic cell, and that lactylated proteins, including a crowd of unique parasite proteins, were involved in a remarkably diverse array of cellular functions. These valuable data will improve our understanding of the evolution of Kla while potentially providing novel therapeutic avenues.

2022-06-09 | PXD031526 | Pride

Histone Kla is regulated by cellular glycolysis

Project description:We have identified a new histone modification, which is derived from glycolysis end product, lactate. By SILAC-MS/MS based quantification, and U-13C6 glucose labeling experiments, we demonstrate that histone Kla is regulated by cellular glycolysis pathway

2019-08-01 | PXD014870 | Pride

Lysine lactylation regulates biofilm formation of streptococcus mutans

Project description:Lactate produced in glycolysis has recently been discovered to modify lysine residues on eukaryotic proteins, a post-translational modification (PTM) called lysine lactylation (Kla). This modification not only participates in regulating gene expression through lactylation of histones, but also impacts the function of non-histone proteins. However, lactylation in prokaryotes has not been reported. Here, we report the identification of 1869 lysine lactylation sites in 465 proteins in the cariogenic organism Streptococcus mutans using a newly developed 4-dimensional label-free quantitative proteomic approach, representing the first Kla dataset in prokaryotes. Combining quantitative analysis, we report that the modification levels of 282 sites from 124 proteins increased by over 1.5-fold, and 80 sites from 52 proteins decreased by over 0.67-fold in the biofilm growth state. These results provide a systematic perspective of the distribution and function of Kla and improve our understanding of the role of lactate in the metabolic regulation of prokaryotes.

2023-08-24 | PXD037027 | Pride

Analysis of proteome refines key molecular reprogramming mechanisms during oil production in Nannochloropsis oceanica

Project description:To examine the mechanisms during oil production and integrate analysis of lactylation in N. oceanica, protein expression profiles were tracked after nitrogen deprivation for three days using 4D label-free proteome method. Under nitrogen deprivation (ND) and nitrogen repletion (NR) cultivation conditions, we mapped proteome of proliferating microalgal cells.

2024-07-03 | PXD038833 | Pride

Staphylococcus aureus LC-MSMS lactylation

Project description:To extensively elucidate protein lactylation (Kla), a proteome-wide analysis of lactylation was carried out in Staphylococcus aureus. Proteins extracted from Staphylococcus aureus were digested by trypsin and anti-lactyl lysine antibody was used to enrich the lactylated peptides, which were determined by following LC-MS/MS analysis.

2024-10-08 | PXD046022 | Pride

Global Proteomic Analysis of Lysine lactylation in HMC3 cells under Normoxia or Hypoxia

Project description:This project carried out a quantitative study of lactylation in HMC3 Cell Line. In order to ensure a high degree of credibility of the results, we used the standard of localization probability>0.75 to filter the authentication data. In this study, a total of 3093 lactylation sites located on 1270 proteins were identified, of which 1601 sites of 751 proteins contain quantitative information. Subsequently, we carried out a systematic bioinformatics analysis of proteins containing quantitative information sites, including protein annotation, functional classification, functional enrichment and cluster analysis based on functional enrichment.

2023-03-28 | PXD028737 | Pride

SILAC experiment quantifying the proteomics of WT and HBO1-KO HeLa

Project description:Lysine lactylation (Kla) links metabolism and gene regulation and plays a key role in multiple biological processes. We report that HBO1 functions as a lysine lactyltransferase to regulate transcription. Quantitative proteomic analysis further revealsed 95 endogenous Kla sites targeted by HBO1, with the majority located on histones.

2024-04-13 | PXD051415 | Pride

Toxoplasma gondii; protein posttranslational modification; lactylation; metabolism; function

Project description:Toxoplasma gondii, a single-celled protozoan parasite (phylum Apicomplexa) and remains the causative pathogen of one of the most wide-spread infectious diseases, toxoplasmosis. To continuously proliferate in warm-blooded animals, this parasite undergoes repeated cycles of invasion, division and induction of host cell rupture. Lactate, which is derived from cellular metabolic pathways, is widely considered not only an energy source in organisms but also a regulatory molecule that participates in gene activation. Lysine lactylation is a new type of protein posttranslational modification (PTM) that was recently associated with chromatin remodeling, but the lysine lactylation of histone and nonhistone proteins has not yet been studied in parasites. To examine the prevalence and function of lactylation in T. gondii parasites, we mapped the lactylation proteome of proliferating tachyzoite cells and found 1,964 lactylation sites on 955 proteins in the T. gondii RH strain. The lactylated proteins were distributed in multiple subcellular compartments and were closely related to a wide variety of biological processes, including mRNA splicing, the citrate cycle (TCA cycle), aminoacyl-tRNA biosynthesis, glyoxylate and dicarboxylate metabolism, glycolysis/gluconeogenesis, oxidative phosphorylation, RNA transport and the HIF-1 signaling pathway. Lysine lactation might regulate numerous cellular processes to aid the establishment of a hospitable environment that allows the survival, replication and dissemination of the parasite. These study offers the first data of the global lactylation proteome and provides a basis for further functional dissection of important proteins associated with T. gondii development and pathogenicity.

2024-04-07 | PXD022700 | Pride

Succinylation in pseudorabies virus infection

Project description:We examined the global succinylation during PRV infection through a 4D label free quantitative proteomics method, which is the conventional separation of the three dimensions of mass-to-charge ratio, retention time, and ion intensity with the inclusion of the ion separation as a fourth dimension. We analyzed the function of some key enzymes that underwent succinylation and determine whether viral proteins undergo succinylation.

2023-03-02 | PXD040521 | Pride