Systematic analysis of lysine malonylation in Streptococcus mutans

Li, Zhengyi; Wu, Qinrui; Zhang, Yixin; Peng, Xian

doi:10.3389/fcimb.2022.1078572

Cited by 3 publications

(2 citation statements)

References 41 publications

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“…Interestingly, mTOR malonylation inhibited the kinase activity of mTOR complex 1, thus hampering angiogenesis and neovascularization [ 46 ]. Furthermore, various research has emphasized the significance of malonylation in metabolism; e.g., Kma proteins are involved in multiple metabolic processes, including RNA degradation, energy metabolism, and the synthesis of various secondary metabolites [ 47 ]. Increased malonylation in cells causes impaired mitochondrial function, fatty acid oxidation, and glucose metabolism [ 41 , 48 ]; therefore, the increased Kma introduced by SIRT5 deficiency was observed to decrease basal mitochondrial respiration and reduce the rate of glycolysis in primary chondrocytes [ 49 ].…”

Section: The Identification and Characterization Of Novel Acylationmentioning

confidence: 99%

A glimpse into novel acylations and their emerging role in regulating cancer metastasis

Shi,

Cui,

Qin

et al. 2024

Cell. Mol. Life Sci.

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Metastatic cancer is a major cause of cancer-related mortality; however, the complex regulation process remains to be further elucidated. A large amount of preliminary investigations focus on the role of epigenetic mechanisms in cancer metastasis. Notably, the posttranslational modifications were found to be critically involved in malignancy, thus attracting considerable attention. Beyond acetylation, novel forms of acylation have been recently identified following advances in mass spectrometry, proteomics technologies, and bioinformatics, such as propionylation, butyrylation, malonylation, succinylation, crotonylation, 2-hydroxyisobutyrylation, lactylation, among others. These novel acylations play pivotal roles in regulating different aspects of energy mechanism and mediating signal transduction by covalently modifying histone or nonhistone proteins. Furthermore, these acylations and their modifying enzymes show promise regarding the diagnosis and treatment of tumors, especially tumor metastasis. Here, we comprehensively review the identification and characterization of 11 novel acylations, and the corresponding modifying enzymes, highlighting their significance for tumor metastasis. We also focus on their potential application as clinical therapeutic targets and diagnostic predictors, discussing the current obstacles and future research prospects.

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Section: The Identification and Characterization Of Novel Acylationmentioning

confidence: 99%

A glimpse into novel acylations and their emerging role in regulating cancer metastasis

Shi,

Cui,

Qin

et al. 2024

Cell. Mol. Life Sci.

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“…Li et al . performed a global protein lysine malonylation (Kmal) analysis of S. mutans and identified a total of 392 malonyllysine sites in 159 proteins [ 66 ]. Among them, proteins (WapA, SpaP, GtfC, Ftf, GbpB) closely related to S. mutans biofilm formation were modified with Kmal, suggesting that Kmal is related to exopolysaccharides synthesis and biofilm formation [ 66 ].…”

Section: Regulation Of S Mutans Biofilm Formation ...mentioning

confidence: 99%

Regulatory mechanisms of exopolysaccharide synthesis and biofilm formation in Streptococcus mutans

Zheng

Jing

Gong

et al. 2023

Journal of Oral Microbiology

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Background Dental caries is a chronic, multifactorial and biofilm-mediated oral bacterial infection affecting almost every age group and every geographical region. Streptococcus mutans is considered an important pathogen responsible for the initiation and development of dental caries. It produces exopolysaccharides in situ to promote the colonization of cariogenic bacteria and coordinate dental biofilm development. Objective The understanding of the regulatory mechanism of S. mutans biofilm formation can provide a theoretical basis for the prevention and treatment of caries. Design At present, an increasing number of studies have identified many regulatory systems in S. mutans that regulate biofilm formation, including second messengers (e.g. c-di-AMP, Ap4A), transcription factors (e.g. EpsR, RcrR, StsR, AhrC, FruR), two-component systems (e.g. CovR, VicR), small RNA (including sRNA0426, srn92532, and srn133489), acetylation modifications (e.g. ActG), CRISPR-associated proteins (e.g. Cas3), PTS systems (e.g. EIIAB), quorum-sensing signaling system (e.g. LuxS), enzymes (including Dex, YidC, CopZ, EzrA, lmrB, SprV, RecA, PdxR, MurI) and small-molecule metabolites. Results This review summarizes the recent progress in the molecular regulatory mechanisms of exopolysaccharides synthesis and biofilm formation in S. mutans .

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A click chemistry-based biorthogonal approach for the detection and identification of protein lysine malonylation for osteoarthritis research

Binoy,

Nanjan,

Chellamuthu

et al. 2024

Preprint

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Lysine malonylation is a post-translational modification where a malonyl group, characterized by a negatively charged carboxylate, is covalently attached to the Ɛ-amino side chain of lysine, influencing protein structure and function. Our laboratory identified Mak upregulation in cartilage under aging and obesity, contributing to osteoarthritis (OA). Current antibody-based detection methods face limitations in identifying Mak targets. Here, we introduce an alkyne-functionalized probe, MA-diyne, which metabolically incorporates into proteins, enabling copper(I) ion-catalyzed click reactions to conjugate labeled proteins with azide-based fluorescent dyes or affinity purification tags. In-gel fluorescence confirms MA-diyne incorporation into proteins across various cell types and species, including mouse chondrocytes, adipocytes, Hek293T cells, and C. elegans. Pull-down experiments identified known Mak proteins such as GAPDH and Aldolase. The extent of MA-diyne modification was higher in Sirtuin 5-deficient cells suggesting these modified proteins are Sirtuin 5 substrates. Pulse-chase experiments confirmed the dynamic nature of protein malonylation. Quantitative proteomics identified 1136 proteins corresponding to 8903 peptides with 429 proteins showing 1-fold increase in labeled group. Sirtuin 5 regulated 374 of these proteins. Pull down of newly identified proteins such as β-actin and Stat3 was also done. This study highlights MA-diyne as a powerful chemical tool to investigate the molecular targets and functions of lysine malonylation in OA conditions.

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Systematic analysis of lysine malonylation in Streptococcus mutans

Cited by 3 publications

References 41 publications

A glimpse into novel acylations and their emerging role in regulating cancer metastasis

A glimpse into novel acylations and their emerging role in regulating cancer metastasis

Regulatory mechanisms of exopolysaccharide synthesis and biofilm formation in Streptococcus mutans

A click chemistry-based biorthogonal approach for the detection and identification of protein lysine malonylation for osteoarthritis research

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