Comprehensive Analysis of Lysine Lactylation in Rice (<i>Oryza sativa</i>) Grains

Meng, Xiaoxi; Baine, Jonathan M; Yan, Tingcai; Shu, Wang

doi:10.1021/acs.jafc.1c00760

Cited by 52 publications

(91 citation statements)

References 46 publications

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“…To define the possible Kla motifs in lactylated proteins, we compared the amino acid sequences surrounding confirmed Kla sites and identified 10 conserved motifs; xxxxxxxxxx_K_xxGxxxxxxx (present in 80 of the 1014 peptides), xxxKxxxxxx_K_xxxxxxxxxx (100 peptides), xxxxxxxxPx_K_xxxxxxxxxx (87 peptides), xxxxxxxxxx_K_xxxxxxxxKx (132 peptides), xxxxxxxxxx_K_xxxxxxKxxx (152 peptides), xxxxxxxxxx_K_xxxxxRxxxx (149 peptides), xxxxxxxxxx_K_xxxxxKxxxx (202 peptides), xxxxxxxxxx_K_x-xxxKxxxxx (240 peptides), xxKxxxxxxx_K_xxxxxxxxxx (325 peptides), and xxxxxxxxxx_K_xxxxxxxKxx (274 peptides) ( Figure 2 A). These motifs differ from those identified in O. sativa and B. cinerea ( Gao et al., 2020 ; Meng et al., 2021 ). Heatmaps of the amino acid sequences surrounding lactylation sites demonstrated that K residues were enriched in the regions from −10 to −3 and from 3 to 10, and that A residues were enriched in the regions from −8 to −1 and from 1 to 6 ( Figure 2 B).…”

Section: Resultscontrasting

confidence: 84%

“…The functions of histone Kla were then explored in mouse embryo fibroblasts (MEFs) ( Li et al., 2020a ), ocular melanoma cells ( Yu et al., 2021 ), and non-small cell lung cancer (NSCLC) cells ( Jiang et al., 2021 ); these studies indicated that Kla has important effects in regulating pluripotency and oncogenesis. Few studies have focused on Kla of non-histone proteins, although such studies have been conducted in Botrytis cinerea and Oryza sativa ( Gao et al., 2020 ; Meng et al., 2021 ). Yang et al.…”

Section: Introductionmentioning

confidence: 99%

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Identification of lysine-lactylated substrates in gastric cancer cells

Yang¹,

Yin²,

Shan³

et al. 2022

iScience

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Section: Resultscontrasting

confidence: 84%

Section: Introductionmentioning

confidence: 99%

Identification of lysine-lactylated substrates in gastric cancer cells

Yang¹,

Yin²,

Shan³

et al. 2022

iScience

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“…Our studies revealed that lactylated proteins were distributed in diverse compartments (especially the mitochondria) and were significantly enriched in energy metabolism processes such as oxidative phosphorylation, glyoxylate and dicarboxylate metabolism, glycolysis/gluconeogenesis, and TCA cycle (Figure 2, Figure S2 and S3). Our results are also in line with previous findings in Trypanosoma brucei and rice, where lactylation is important for gene transcription and central carbon metabolism [48,49]. We therefore focused on the link between lactylation and the processes of energy metabolism.…”

Section: Discussionsupporting

confidence: 91%

Protein Lactylation and Metabolic Regulation of the Zoonotic Parasite Toxoplasma gondii

Yin

Jiang

Cheng

et al. 2022

Preprint

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The biology of Toxoplasma gondii, the causative pathogen of one of the most wide-spread parasitic diseases remains poorly understood. Lactate, which is derived from glucose metabolic pathways, is considered to be not only an energy source in a variety of organisms including Toxoplasma gondii, but also a regulatory molecule that participates in gene activation and protein functioning. Lysine lactylation is a type of posttranslational modifications (PTMs) that was recently associated with chromatin remodeling, but lysine lactylation of histone and non-histone proteins has not yet been studied in T. gondii. To examine the prevalence and function of lactylation in T. gondii parasites, we mapped the lactylome of proliferating tachyzoite cells and found 1964 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, glycolysis, aminoacyl-tRNA biosynthesis, RNA transport, and multiple signaling pathways. We also performed chromatin immunoprecipitation sequencing (ChIP-seq) analysis with a lactylation specific antibody, the results revealed that histone H4K12la and H3K14la were enriched in the promoter and exon regions of Toxoplasma gondii genes associated with microtubule-based movement and cell invasion. We further confirmed the de-lactylase activity of histone deacetylase TgHDACs 2, 3, and 4, and that treatment with anti-histone acetyltransferase (TgMYST-A) antibodies profoundly reduced protein lactylation in the parasites. This study offers the first dataset of the global lactylation proteome and provides a basis for further dissection of the functional biology of Toxoplasma gondii.

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“…The lysine residue is one of the most frequently modified targets due to its function in the organization of protein spatial structure. Lysine lactylation (Kla) is a novel PTM that has been identified on both histone and nonhistone proteins in several organisms, including humans [ 3 , 4 ], mice [ 5 ], rice ( Oryza sativa ) [ 6 ], plant fungal pathogen ( Botrytis cinerea ) [ 7 ] and parasitic protozoan ( Trypanosoma brucei ) [ 8 ]. During this modification, the 72.021-Da of the l -lactate-derived lactyl group is covalently attached onto lysine residues via an enzymatic reaction mediated by the acetyl transferase p300 [ 3 ].…”

Section: Introductionmentioning

confidence: 99%

Systematic identification of the lysine lactylation in the protozoan parasite Toxoplasma gondii

Zhao

Liu

et al. 2022

Parasites Vectors

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Background Lysine lactylation (Kla) is a novelposttranslational modification (PTM) identified in histone and nonhistone proteins of several eukaryotic cells that directly activates gene expression and DNA replication. However, very little is known about the scope and cellular distribution of Kla in apicomplexan parasites despite its significance in public and animal health care. Methods Toxoplasma gondii, the causative agent of toxoplasmosis, is an obligate intracellular apicomplexan parasite that can infect different nucleated cell types of animals and humans. We used this parasite as a model organism and extracted the total protein of tachyzoites to produce the first global lysine lactylome profile of T. gondii through liquid chromatography–tandem mass spectrometry. We also investigated the level and localization of the Kla protein in T. gondii using western blotting and the indirect fluorescent antibody test (IFA), respectively. Results A total of 983 Kla sites occurring on 523 lactylated proteins were identified in the total protein extracted from Toxoplasma tachyzoites, the acute toxoplasmosis-causing stage. Bioinformatics analysis revealed that the lactylated proteins were evolutionarily conserved and involved in a wide variety of cellular functions, such as energy metabolism, gene regulation and protein biosynthesis. Subcellular localization analysis and IFA results further revealed that most of the lactylated T. gondii proteins were localized in the nucleus, indicating the potential impact of Kla on gene regulation in the T. gondii model. Notably, an extensive batch of parasite-specific proteins unique to phylum Apicomplexa is lactylated in T. gondii. Conclusions This study revealed that Kla is widespread in early dividing eukaryotic cells. Lactylated proteins, including a batch of unique parasite proteins, are involved in a remarkably diverse array of cellular functions. These valuable data will improve our understanding of the evolution of Kla and potentially provide the basis for developing novel therapeutic avenues. Graphical Abstract

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Comprehensive Analysis of Lysine Lactylation in Rice (Oryza sativa) Grains

Cited by 52 publications

References 46 publications

Identification of lysine-lactylated substrates in gastric cancer cells

Identification of lysine-lactylated substrates in gastric cancer cells

Protein Lactylation and Metabolic Regulation of the Zoonotic Parasite Toxoplasma gondii

Systematic identification of the lysine lactylation in the protozoan parasite Toxoplasma gondii

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