Bacterial protein acetylation and its role in cellular physiology and metabolic regulation

Liu, Min; Guo, Likun; Fu, Yingxin; Huo, Meitong; Qi, Qingsheng; Zhao, Guang

doi:10.1016/j.biotechadv.2021.107842

Cited by 32 publications

(29 citation statements)

References 121 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Together with this finding, proteome analysis also revealed that two NAD-dependent deacetylases, enzymes that catalyze protein deacetylation, are strongly induced in sinigrin containing medium (Table 1 ). Protein acetylation/deacetylation is a hot topic in recent years because it is an evolutionarily conserved post-translational modification that affects enzyme activity, metabolic flux, and many important biochemical processes, but the regulatory mechanisms have not been well characterized in bacteria 28 . Focusing on these deacetylases may lead to a better understanding of the response mechanisms of lactic acid bacteria to the presence of bioactive phytochemicals such as sinigrin or AITC.…”

Section: Discussionmentioning

confidence: 99%

Enzyme systems involved in glucosinolate metabolism in Companilactobacillus farciminis KB1089

Watanabe

Usami

Kishino

et al. 2021

Sci Rep

View full text Add to dashboard Cite

Cruciferous vegetables are rich sources of glucosinolates (GSLs). GSLs are degraded into isothiocyanates, which are potent anticarcinogens, by human gut bacteria. However, the mechanisms and enzymes involved in gut bacteria-mediated GSL metabolism are currently unclear. This study aimed to elucidate the enzymes involved in GSL metabolism in lactic acid bacteria, a type of gut bacteria. Companilactobacillus farciminis KB1089 was selected as a lactic acid bacteria strain model that metabolizes sinigrin, which is a GSL, into allylisothiocyanate. The sinigrin-metabolizing activity of this strain is induced under glucose-absent and sinigrin-present conditions. A quantitative comparative proteomic analysis was conducted and a total of 20 proteins that were specifically expressed in the induced cells were identified. Three candidate proteins, β-glucoside-specific IIB, IIC, IIA phosphotransferase system (PTS) components (CfPttS), 6-phospho-β-glucosidase (CfPbgS) and a hypothetical protein (CfNukS), were suspected to be involved in sinigrin-metabolism and were thus investigated further. We hypothesize a pathway for sinigrin degradation, wherein sinigrin is taken up and phosphorylated by CfPttS, and subsequently, the phosphorylated entity is degraded by CfPbgS. As expression of both pttS and pbgS genes clearly gave Escherichia coli host strain sinigrin converting activity, these genes were suggested to be responsible for sinigrin degradation. Furthermore, heterologous expression analysis using Lactococcus lactis suggested that CfPttS was important for sinigrin degradation and CfPbgS degraded phosphorylated sinigrin.

show abstract

Section: Discussionmentioning

confidence: 99%

Enzyme systems involved in glucosinolate metabolism in Companilactobacillus farciminis KB1089

Watanabe

Usami

Kishino

et al. 2021

Sci Rep

View full text Add to dashboard Cite

show abstract

“…In order to adapt a changing environment, cells undergo complex regulations at different levels. Among them, posttranslational modification (PTM) can covalently modify amino acid by biochemical mechanism to make the protein structure more complex and the regulatory effect more precise ( Liu et al, 2021 ). Protein lysine acetylation is a highly conserved PTM from bacteria to higher animals ( Hentchel and Escalante-Semerena, 2015 ; VanDrisse and Escalante-Semerena, 2019 ).…”

Section: Introductionmentioning

confidence: 99%

“…In nonenzymatic acetylation, an acetyl group from acetyl phosphate (AcP) direct transfers to protein lysine residues. AcP- mediated nonenzymatic acetylation is the primary mechanism of E. coli ( Liu et al, 2021 ).…”

Section: Introductionmentioning

confidence: 99%

“…In recent decades, many bacterial acetylated proteins were constantly discovered with the development of high-affinity immune separation and nano-HPLC/MS/MS ( Yu et al, 2008 ; Zhang et al, 2009 ; Zhang et al, 2013 ; Kuhn et al, 2014 ). Lysine acetylation is abundant in bacteria, affecting the cellular physiology and metabolism ( Wang, 2010 ; Liu et al, 2021 ). Thus, lysine acetylation may become a promising tool in metabolic engineering.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Lysine acetylation of Escherichia coli lactate dehydrogenase regulates enzyme activity and lactate synthesis

Liu

Huo

Liu

et al. 2022

Front. Bioeng. Biotechnol.

Self Cite

View full text Add to dashboard Cite

As an evolutionarily conserved posttranslational modification, protein lysine acetylation plays important roles in many physiological and metabolic processes. However, there are few reports about the applications of lysine acetylation in metabolic regulations. Lactate is a main byproduct in microbial fermentation, and itself also an important bulk chemical with considerable commercial values in many fields. Lactate dehydrogenase (LdhA) is the key enzyme catalyzing lactate synthesis from pyruvate. Here, we reported that Escherichia coli LdhA can be acetylated and the acetylated lysine sites were identified by mass spectrometry. The effects and regulatory mechanisms of acetylated sites on LdhA activity were characterized. Finally, lysine acetylation was successfully used to regulate the lactate synthesis. LdhA (K9R) mutant overexpressed strain improved the lactate titer and glucose conversion efficiency by 1.74 folds than that of wild-type LdhA overexpressed strain. LdhA (K154Q-K248Q) mutant can inhibit lactate accumulation and improve 3HP production. Our study established a paradigm for lysine acetylation in lactate synthesis regulation and suggested that lysine acetylation may be a promising strategy to improve the target production and conversion efficiency in microbial synthesis. The application of lysine acetylation in regulating lactate synthesis also provides a reference for the treatment of lactate-related diseases.

show abstract

“…In some pathogens, lysine acetylation modification affects bacterial virulence by regulating the activity of key factors, such as acetylation regulating protein stability and DNA-binding ability of HilD to modulate Salmonella Typhimurium virulence ( 18 ), acetylation of lysine 201 inhibits the DNA-binding ability of PhoP to regulate Salmonella virulence ( 19 ), acetylation of PhoP K88 is involved in regulating Salmonella virulence ( 20 ), acetylation is involved in Salmonella enterica Serovar Typhimurium Virulence and so on ( 15 , 21 ). Furthermore, lysine acetylation can regulate the activity of various metabolic enzymes, such as glyceraldehyde phosphate dehydrogenase, isocitrate lyase, isocitrate dehydrogenase kinase/phosphatase, isocitrate dehydrogenase, malate dehydrogenase citrate synthase ( 22 – 25 ). This suggests that acetylation modifications may play an important role in bacterial.…”

Section: Introductionmentioning

confidence: 99%

Characterizing the Effect of the Lysine Deacetylation Modification on Enzyme Activity of Pyruvate Kinase I and Pathogenicity of Vibrio alginolyticus

Wang²,

Wang³

et al. 2022

Front. Vet. Sci.

View full text Add to dashboard Cite

Pyruvate kinase I (PykF) is one of the key enzymes of glycolysis and plays a crucial role in bacterial metabolism. Several acetylation sites of Vibrio alginolyticus PykF were reported in previous studies and then 11 sites were first verified in this study, however, the specific roles of PykF acetylation remains unclear. Overlap-PCR and homologous recombination were implied to delete V. alginolyticus pykF gene and constructed complementary strains of site-directed mutagenesis for the further research focus on the deacetylation regulation on PykF. The results showed that the pyruvate kinase activity was sharply suppressed in the deacetylation status of K52, K68, and K317 of PykF, as well as the extracellular protease activity was significantly decreased in the deacetylation status of K52 and K68, but not induced with K317. Moreover, the growth rates of V. alginolyticus were not influenced with these three deacetylation sites. The ΔpykF mutant exhibited a 6-fold reduction in virulence to zebrafish. Site-directed mutations of K52R and K68R also showed reduced virulence while mutations of K317R didn't. The in vitro experiments showed that PykF was acetylated by acetyl phosphate (AcP), with the increase of incubation time by AcP, the acetylation level of PykF increased while the enzyme activity of PykF decreased correspondingly. Besides, PykF was deacetylated by CobB deacetylase and in result that the deacetylation was significantly down-regulated while the pyruvate kinase activity of PykF increased. Moreover, deletion of cobB gene had no significant difference in pyruvate kinase activity. These results confirm that CobB can regulate the acetylation level and pyruvate kinase activity of PykF. In summary, the results of this study provide a theoretical basis for further understanding of the deacetylation modification of PykF. It provides a new idea for the prevention and cure of vibriosis.

show abstract

Bacterial protein acetylation and its role in cellular physiology and metabolic regulation

Cited by 32 publications

References 121 publications

Enzyme systems involved in glucosinolate metabolism in Companilactobacillus farciminis KB1089

Enzyme systems involved in glucosinolate metabolism in Companilactobacillus farciminis KB1089

Lysine acetylation of Escherichia coli lactate dehydrogenase regulates enzyme activity and lactate synthesis

Characterizing the Effect of the Lysine Deacetylation Modification on Enzyme Activity of Pyruvate Kinase I and Pathogenicity of Vibrio alginolyticus

Contact Info

Product

Resources

About