Acetylome Analysis Reveals Diverse Functions of Lysine Acetylation in Mycobacterium tuberculosis

Liu, Fengying; Yang, Mingkun; Wang, Xude; Yang, Shimei; Gu, Jing; Zhou, Jie; Zhang, Xian-En; Deng, Jiao-Yu; Ge, Feng

doi:10.1074/mcp.m114.041962

Cited by 142 publications

(191 citation statements)

References 75 publications

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“…Fatty acid biosynthesis in this organism has been shown to play a role in colony morphology and biofilm formation. The authors of that study demonstrated that deletion of the sirtuin deacetylase in this organism (MRA_1161) resulted in a more granular morphology, a decrease in biofilm formation, and increased resistance to heat stress (143). These studies further support the hypothesis that RLA is a mechanism for protection against environmental stresses.…”

Section: Cellular Stress and Rlasupporting

confidence: 70%

“…Specifically, the function of the proteins identified as acetylation targets has not been analyzed in vitro to identify the modifying enzymes or whether or not acety- Ac , number of identified acetylated proteins; % Total Ac , percentage of acetylated proteins of the entire proteome; N, no; Y, yes. *, values are different than those previously reported; however, the values listed reflect the available data that were obtained from supplementary information from the cited references (28,142,143,(153)(154)(155)(156)(157)(158)(159)(160)(161). The percent scale at the top should be used to estimate the percentage of acetylated proteins in each of the categories within any given microorganism shown.…”

Section: Bacterial Acetylome Studiesmentioning

confidence: 62%

“…A recent acetylome study of M. tuberculosis identified that 10% of the enzymes involved in fatty acid biosynthesis were acetylated (143). Fatty acid biosynthesis in this organism has been shown to play a role in colony morphology and biofilm formation.…”

Section: Cellular Stress and Rlamentioning

confidence: 99%

“…8A). These global studies have been extended to archaea (N-terminal acetylation) (140), bacteria (141)(142)(143), plants (144), parasites (145,146), and humans (147), helping cement the fundamental principles and contributions of acetylation to cellular physiology. Such global studies consistently suggest that acetylation controls diverse cellular processes, including metabolism, transcription, translation, and cell structure.…”

Section: High-throughput Identification Of Acetylated Proteins Globalmentioning

confidence: 99%

“…Bacterial acetylomes have been characterized in E. coli (141,142), S. enterica (153), Bacillus subtilis (154), Erwinia amylovora (155), R. palustris (28), Staphylococcus aureus (156), Geobacillus kaustophilus (157), Vibrio parahaemolyticus (158), Thermus thermophilus (159), M. tuberculosis (143), Mycoplasma pneumoniae (160), and Streptomyces roseosporus (161). These studies have identified a range of 62 to 667 putatively acetylated proteins per organism, with the majority of acetylated proteins being involved in central metabolism and translation (141,156,158) (Fig.…”

Section: Bacterial Acetylome Studiesmentioning

confidence: 99%

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Acylation of Biomolecules in Prokaryotes: a Widespread Strategy for the Control of Biological Function and Metabolic Stress

Hentchel

Escalante‐Semerena

2015

Microbiol Mol Biol Rev

163

175

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SUMMARY Acylation of biomolecules (e.g., proteins and small molecules) is a process that occurs in cells of all domains of life and has emerged as a critical mechanism for the control of many aspects of cellular physiology, including chromatin maintenance, transcriptional regulation, primary metabolism, cell structure, and likely other cellular processes. Although this review focuses on the use of acetyl moieties to modify a protein or small molecule, it is clear that cells can use many weak organic acids (e.g., short-, medium-, and long-chain mono- and dicarboxylic aliphatics and aromatics) to modify a large suite of targets. Acetylation of biomolecules has been studied for decades within the context of histone-dependent regulation of gene expression and antibiotic resistance. It was not until the early 2000s that the connection between metabolism, physiology, and protein acetylation was reported. This was the first instance of a metabolic enzyme (acetyl coenzyme A [acetyl-CoA] synthetase) whose activity was controlled by acetylation via a regulatory system responsive to physiological cues. The above-mentioned system was comprised of an acyltransferase and a partner deacylase. Given the reversibility of the acylation process, this system is also referred to as r eversible l ysine a cylation (RLA). A wealth of information has been obtained since the discovery of RLA in prokaryotes, and we are just beginning to visualize the extent of the impact that this regulatory system has on cell function.

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Section: Cellular Stress and Rlasupporting

confidence: 70%

Section: Bacterial Acetylome Studiesmentioning

confidence: 62%

Section: Cellular Stress and Rlamentioning

confidence: 99%

Section: High-throughput Identification Of Acetylated Proteins Globalmentioning

confidence: 99%

Section: Bacterial Acetylome Studiesmentioning

confidence: 99%

See 3 more Smart Citations

Acylation of Biomolecules in Prokaryotes: a Widespread Strategy for the Control of Biological Function and Metabolic Stress

Hentchel

Escalante‐Semerena

2015

Microbiol Mol Biol Rev

163

175

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Biochemical, structural, and functional studies reveal that MAB_4324c from Mycobacterium abscessus is an active tandem repeat N‐acetyltransferase

et al. 2022

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Mycobacterium abscessus is a pathogenic non‐tuberculous mycobacterium that possesses an intrinsic drug resistance profile. Several N‐acetyltransferases mediate drug resistance and/or participate in M. abscessus virulence. Mining the M. abscessus genome has revealed genes encoding additional N‐acetyltransferases whose functions remain uncharacterized, among them MAB_4324c. Here, we showed that the purified MAB_4324c protein is a N‐acetyltransferase able to acetylate small polyamine substrates. The crystal structure of MAB_4324c was solved at high resolution in complex with its cofactor, revealing the presence of two GCN5‐related N‐acetyltransferase domains and a cryptic binding site for NADPH. Genetic studies demonstrate that MAB_4324c is not essential for in vitro growth of M. abscessus; however, overexpression of the protein enhanced the uptake and survival of M. abscessus in THP‐1 macrophages.

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Altered acetylation and succinylation profiles in Corynebacterium glutamicum in response to conditions inducing glutamate overproduction

et al. 2015

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The bacterium Corynebacterium glutamicum is utilized during industrial fermentation to produce amino acids such as l‐glutamate. During l‐glutamate fermentation, C. glutamicum changes the flux of central carbon metabolism to favor l‐glutamate production, but the molecular mechanisms that explain these flux changes remain largely unknown. Here, we found that the profiles of two major lysine acyl modifications were significantly altered upon glutamate overproduction in C. glutamicum; acetylation decreased, whereas succinylation increased. A label‐free semi‐quantitative proteomic analysis identified 604 acetylated proteins with 1328 unique acetylation sites and 288 succinylated proteins with 651 unique succinylation sites. Acetylation and succinylation targeted enzymes in central carbon metabolic pathways that are directly related to glutamate production, including the 2‐oxoglutarate dehydrogenase complex (ODHC), a key enzyme regulating glutamate overproduction. Structural mapping revealed that several critical lysine residues in the ODHC components were susceptible to acetylation and succinylation. Furthermore, induction of glutamate production was associated with changes in the extent of acetylation and succinylation of lysine, suggesting that these modifications may affect the activity of enzymes involved in glutamate production. Deletion of phosphotransacetylase decreased the extent of protein acetylation in nonproducing condition, suggesting that acetyl phosphate‐dependent acetylation is active in C. glutamicum. However, no effect was observed on the profiles of acetylation and succinylation in glutamate‐producing condition upon disruption of acetyl phosphate metabolism or deacetylase homologs. It was considered likely that the reduced acetylation in glutamate‐producing condition may reflect metabolic states where the flux through acid‐producing pathways is very low, and substrates for acetylation do not accumulate in the cell. Succinylation would occur more easily than acetylation in such conditions where the substrates for both acetylation and succinylation are limited. This is the first study investigating the acetylome and succinylome of C. glutamicum, and it provides new insight into the roles of acyl modifications in C. glutamicum biology.

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Acetylome Analysis Reveals Diverse Functions of Lysine Acetylation in Mycobacterium tuberculosis

Cited by 142 publications

References 75 publications

Acylation of Biomolecules in Prokaryotes: a Widespread Strategy for the Control of Biological Function and Metabolic Stress

Acylation of Biomolecules in Prokaryotes: a Widespread Strategy for the Control of Biological Function and Metabolic Stress

Biochemical, structural, and functional studies reveal that MAB_4324c from Mycobacterium abscessus is an active tandem repeat N‐acetyltransferase

Altered acetylation and succinylation profiles in Corynebacterium glutamicum in response to conditions inducing glutamate overproduction

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