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Saori Kosono - One of the best experts on this subject based on the ideXlab platform.
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Protein Acetylation on 2-isopropylmalate synthase from Thermus thermophilus HB27
Extremophiles, 2019Co-Authors: Ayako Yoshida, Minoru Yoshida, Tomohisa Kuzuyama, Makoto Nishiyama, Saori KosonoAbstract:Protein lysine N ^ε-Acetylation is one of the important factors regulating cellular metabolism. We performed a proteomic analysis to identify acetylated Proteins in the extremely thermophilic bacterium, Thermus thermophilus HB27. A total of 335 unique acetylated lysine residues, including many metabolic enzymes and ribosomal Proteins, were identified in 208 Proteins. Enzymes involved in amino acid metabolism were the most abundant among acetylated metabolic Proteins. 2-Isopropylmalate synthase (IPMS), which catalyzes the first step in leucine biosynthesis, was acetylated at four lysine residues. Acetylation-mimicking mutations at Lys332 markedly decreased IPMS activity in vitro, suggesting that Lys332, which is located in subdomain II, plays a regulatory role in IPMS activity. We also investigated the Acetylation-deAcetylation mechanism of IPMS and revealed that it was acetylated non-enzymatically by acetyl-CoA and deacetylated enzymatically by TT_C0104. The present results suggest that leucine biosynthesis is regulated by post-translational Protein modifications, in addition to feedback inhibition/repression, and that metabolic enzymes are regulated by Protein Acetylation in T. thermophilus .
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Protein Acetylation on 2-isopropylmalate synthase from Thermus thermophilus HB27.
Extremophiles : life under extreme conditions, 2019Co-Authors: Ayako Yoshida, Minoru Yoshida, Tomohisa Kuzuyama, Makoto Nishiyama, Saori KosonoAbstract:Protein lysine Ne-Acetylation is one of the important factors regulating cellular metabolism. We performed a proteomic analysis to identify acetylated Proteins in the extremely thermophilic bacterium, Thermus thermophilus HB27. A total of 335 unique acetylated lysine residues, including many metabolic enzymes and ribosomal Proteins, were identified in 208 Proteins. Enzymes involved in amino acid metabolism were the most abundant among acetylated metabolic Proteins. 2-Isopropylmalate synthase (IPMS), which catalyzes the first step in leucine biosynthesis, was acetylated at four lysine residues. Acetylation-mimicking mutations at Lys332 markedly decreased IPMS activity in vitro, suggesting that Lys332, which is located in subdomain II, plays a regulatory role in IPMS activity. We also investigated the Acetylation-deAcetylation mechanism of IPMS and revealed that it was acetylated non-enzymatically by acetyl-CoA and deacetylated enzymatically by TT_C0104. The present results suggest that leucine biosynthesis is regulated by post-translational Protein modifications, in addition to feedback inhibition/repression, and that metabolic enzymes are regulated by Protein Acetylation in T. thermophilus.
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Protein Acetylation involved in streptomycin biosynthesis in Streptomyces griseus.
Journal of proteomics, 2016Co-Authors: Yuji Ishigaki, Genki Akanuma, Minoru Yoshida, Sueharu Horinouchi, Saori Kosono, Yasuo OhnishiAbstract:Abstract Protein Acetylation, the reversible addition of an acetyl group to lysine residues, is a Protein post-translational modification ubiquitous in living cells. Although the involvement of Protein Acetylation in the regulation of primary metabolism has been revealed, the function of Protein Acetylation is largely unknown in secondary metabolism. Here, we characterized Protein Acetylation in Streptomyces griseus , a streptomycin producer. Protein Acetylation was induced in the stationary and sporulation phases in liquid and solid cultures, respectively, in S. griseus . By comprehensive acetylome analysis, we identified 134 acetylated Proteins with 162 specific acetylated sites. Acetylation was found in Proteins related to primary metabolism and translation, as in other bacteria. However, StrM, a deoxysugar epimerase involved in streptomycin biosynthesis, was identified as a highly acetylated Protein by 2-DE-based proteomic analysis. The Lys70 residue, which is critical for the enzymatic activity of StrM, was the major Acetylation site. Thus, Acetylation of Lys70 was presumed to abolish enzymatic activity of StrM. In accordance with this notion, an S. griseus mutant producing the Acetylation-mimic K70Q StrM hardly produced streptomycin, though the K70Q mutation apparently decreased the stability of StrM. A putative lysine acetyltransferase (KAT) SGR1683 in S. griseus , as well as the Escherichia coli KAT YfiQ, acetylated Lys70 of StrM in vitro . Furthermore, absolute quantification analysis estimated that 13% of StrM molecules were acetylated in mycelium grown in solid culture for 3 days. These results indicate that StrM Acetylation is of biological significance. We propose that StrM Acetylation functions as a limiter of streptomycin biosynthesis in S. griseus . Biological significance Protein Acetylation has been extensively studied not only in eukaryotes, but also in prokaryotes. The acetylome has been analyzed in more than 14 bacterial species. Here, by comprehensive acetylome analysis, we showed that Acetylation was found in Proteins related to primary metabolism and translation in Streptomyces griseus , similarly to other bacteria. However, five Proteins involved in secondary metabolism were also identified as acetylated Proteins; these Proteins are enzymes in the biosynthesis of streptomycin (StrB1 and StrS), grixazone (GriF), a nonribosomal peptide (NRPS1–2), and a siderophore (AlcC). Additionally, StrM in streptomycin biosynthesis was identified as a highly acetylated Protein by 2-DE-based proteomic analysis; approximately 13% of StrM molecules were acetylated. The Acetylation occurs at Lys70 to abolish the enzymatic activity of StrM, suggesting that StrM Acetylation functions as a limiter of streptomycin biosynthesis in S. griseus . This is the first detailed analysis of Protein Acetylation of an enzyme involved in secondary metabolism.
Yu-feng Yao - One of the best experts on this subject based on the ideXlab platform.
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Protein Acetylation and Its Role in Bacterial Virulence.
Trends in microbiology, 2017Co-Authors: Jie Ren, Yu Sang, Yu-feng YaoAbstract:Protein Acetylation is a universal post-translational modification which is found in both eukaryotes and prokaryotes. This process is achieved enzymatically by the Protein acetyltransferase Pat, and nonenzymatically by metabolic intermediates (e.g., acetyl phosphate) in bacteria. Protein Acetylation plays a role in bacterial chemotaxis, metabolism, DNA replication, and other cellular processes. Recently, accumulating evidence has suggested that Protein Acetylation might be involved in bacterial virulence because a number of bacterial virulence factors are acetylated. In this review, we summarize the progress in understanding bacterial Protein Acetylation and discuss how it mediates bacterial virulence.
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Protein Acetylation Is Involved in Salmonella enterica Serovar Typhimurium Virulence.
The Journal of infectious diseases, 2016Co-Authors: Yu Sang, Jie Ren, Jing Tao, Yu-feng YaoAbstract:Salmonella causes a range of diseases in different hosts, including enterocolitis and systemic infection. Lysine Acetylation regulates many eukaryotic cellular processes, but its function in bacteria is largely unexplored. The acetyltransferase Pat and NAD(+)-dependent deacetylase CobB are involved in the reversible Protein Acetylation in Salmonella Typhimurium. Here, we used cell and animal models to evaluate the virulence of pat and cobB deletion mutants in S. Typhimurium and found that pat is critical for bacterial intestinal colonization and systemic infection. Next, to understand the underlying mechanism, genome-wide transcriptome was analyzed. RNA sequencing data showed that the expression of Salmonella pathogenicity island 1 (SPI-1) is partially dependent on pat In addition, we found that HilD, a key transcriptional regulator of SPI-1, is a substrate of Pat. The Acetylation of HilD by Pat maintained HilD stability and was essential for the transcriptional activation of HilA. Taken together, these results suggest that a Protein Acetylation system regulates SPI-1 expression by controlling HilD in a posttranslational manner to mediate S. Typhimurium virulence.
Willy V. Bienvenut - One of the best experts on this subject based on the ideXlab platform.
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Dual lysine and N-terminal acetyltransferases reveal the complexity underpinning Protein Acetylation
Molecular Systems Biology, 2020Co-Authors: Willy V. Bienvenut, Annika Brünje, Jean-baptiste Boyer, Jens S. Mühlenbeck, Gautier Bernal, Ines Lassowskat, Cyril Dian, Eric Linster, Trinh Dinh, Minna KoskelaAbstract:Protein Acetylation is a highly frequent Protein modification. However, comparatively little is known about its enzymatic machinery. N-a-Acetylation (NTA) and e-lysine Acetylation (KA) are known to be catalyzed by distinct families of enzymes (NATs and KATs, respectively), although the possibility that the same GCN5-related N-acetyltransferase (GNAT) can perform both functions has been debated. Here, we discovered a new family of plastid-localized GNATs, which possess a dual specificity. All characterized GNAT family members display a number of unique features. Quantitative mass spectrometry analyses revealed that these enzymes exhibit both distinct KA and relaxed NTA speci-ficities. Furthermore, inactivation of GNAT2 leads to significant NTA or KA decreases of several plastid Proteins, while Proteins of other compartments were unaffected. The data indicate that these enzymes have specific Protein targets and likely display partly redundant selectivity, increasing the robustness of the Acetylation process in vivo. In summary, this study revealed a new layer of complexity in the machinery controlling this prevalent modification and suggests that other eukaryotic GNATs may also possess these previously underappreciated broader enzy-matic activities.
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Dual lysine and N‐terminal acetyltransferases reveal the complexity underpinning Protein Acetylation
Molecular Systems Biology, 2020Co-Authors: Willy V. Bienvenut, Annika Brünje, Jean-baptiste Boyer, Jens S. Mühlenbeck, Gautier Bernal, Ines Lassowskat, Cyril Dian, Eric Linster, Trinh Dinh, Minna KoskelaAbstract:Protein Acetylation is a highly frequent Protein modification. However, comparatively little is known about its enzymatic machinery. N-a-Acetylation (NTA) and e-lysine Acetylation (KA) are known to be catalyzed by distinct families of enzymes (NATs and KATs, respectively), although the possibility that the same GCN5-related N-acetyltransferase (GNAT) can perform both functions has been debated. Here, we discovered a new family of plastid-localized GNATs, which possess a dual specificity. All characterized GNAT family members display a number of unique features. Quantitative mass spectrometry analyses revealed that these enzymes exhibit both distinct KA and relaxed NTA speci-ficities. Furthermore, inactivation of GNAT2 leads to significant NTA or KA decreases of several plastid Proteins, while Proteins of other compartments were unaffected. The data indicate that these enzymes have specific Protein targets and likely display partly redundant selectivity, increasing the robustness of the Acetylation process in vivo. In summary, this study revealed a new layer of complexity in the machinery controlling this prevalent modification and suggests that other eukaryotic GNATs may also possess these previously underappreciated broader enzy-matic activities.
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Dual lysine and N-terminal acetyltransferases reveal the complexity underpinning Protein Acetylation
Molecular Systems Biology, 2020Co-Authors: Willy V. Bienvenut, Annika Brünje, Jean-baptiste Boyer, Jens S. Mühlenbeck, Gautier Bernal, Ines Lassowskat, Cyril Dian, Eric Linster, Trinh V. Dinh, Minna M. KoskelaAbstract:Protein Acetylation is a highly frequent Protein modification. However, comparatively little is known about its enzymatic machinery. N-α-Acetylation (NTA) and ε-lysine Acetylation (KA) are known to be catalyzed by distinct families of enzymes (NATs and KATs, respectively), although the possibility that the same GCN5-related N-acetyltransferase (GNAT) can perform both functions has been debated. Here, we discovered a new family of plastid-localized GNATs, which possess a dual specificity. All characterized GNAT family members display a number of unique features. Quantitative mass spectrometry analyses revealed that these enzymes exhibit both distinct KA and relaxed NTA specificities. Furthermore, inactivation of GNAT2 leads to significant NTA or KA decreases of several plastid Proteins, while Proteins of other compartments were unaffected. The data indicate that these enzymes have specific Protein targets and likely display partly redundant selectivity, increasing the robustness of the Acetylation process in vivo. In summary, this study revealed a new layer of complexity in the machinery controlling this prevalent modification and suggests that other eukaryotic GNATs may also possess these previously underappreciated broader enzymatic activities.
Minna Koskela - One of the best experts on this subject based on the ideXlab platform.
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Dual lysine and N-terminal acetyltransferases reveal the complexity underpinning Protein Acetylation
Molecular Systems Biology, 2020Co-Authors: Willy V. Bienvenut, Annika Brünje, Jean-baptiste Boyer, Jens S. Mühlenbeck, Gautier Bernal, Ines Lassowskat, Cyril Dian, Eric Linster, Trinh Dinh, Minna KoskelaAbstract:Protein Acetylation is a highly frequent Protein modification. However, comparatively little is known about its enzymatic machinery. N-a-Acetylation (NTA) and e-lysine Acetylation (KA) are known to be catalyzed by distinct families of enzymes (NATs and KATs, respectively), although the possibility that the same GCN5-related N-acetyltransferase (GNAT) can perform both functions has been debated. Here, we discovered a new family of plastid-localized GNATs, which possess a dual specificity. All characterized GNAT family members display a number of unique features. Quantitative mass spectrometry analyses revealed that these enzymes exhibit both distinct KA and relaxed NTA speci-ficities. Furthermore, inactivation of GNAT2 leads to significant NTA or KA decreases of several plastid Proteins, while Proteins of other compartments were unaffected. The data indicate that these enzymes have specific Protein targets and likely display partly redundant selectivity, increasing the robustness of the Acetylation process in vivo. In summary, this study revealed a new layer of complexity in the machinery controlling this prevalent modification and suggests that other eukaryotic GNATs may also possess these previously underappreciated broader enzy-matic activities.
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Dual lysine and N‐terminal acetyltransferases reveal the complexity underpinning Protein Acetylation
Molecular Systems Biology, 2020Co-Authors: Willy V. Bienvenut, Annika Brünje, Jean-baptiste Boyer, Jens S. Mühlenbeck, Gautier Bernal, Ines Lassowskat, Cyril Dian, Eric Linster, Trinh Dinh, Minna KoskelaAbstract:Protein Acetylation is a highly frequent Protein modification. However, comparatively little is known about its enzymatic machinery. N-a-Acetylation (NTA) and e-lysine Acetylation (KA) are known to be catalyzed by distinct families of enzymes (NATs and KATs, respectively), although the possibility that the same GCN5-related N-acetyltransferase (GNAT) can perform both functions has been debated. Here, we discovered a new family of plastid-localized GNATs, which possess a dual specificity. All characterized GNAT family members display a number of unique features. Quantitative mass spectrometry analyses revealed that these enzymes exhibit both distinct KA and relaxed NTA speci-ficities. Furthermore, inactivation of GNAT2 leads to significant NTA or KA decreases of several plastid Proteins, while Proteins of other compartments were unaffected. The data indicate that these enzymes have specific Protein targets and likely display partly redundant selectivity, increasing the robustness of the Acetylation process in vivo. In summary, this study revealed a new layer of complexity in the machinery controlling this prevalent modification and suggests that other eukaryotic GNATs may also possess these previously underappreciated broader enzy-matic activities.
Minoru Yoshida - One of the best experts on this subject based on the ideXlab platform.
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Protein Acetylation on 2-isopropylmalate synthase from Thermus thermophilus HB27
Extremophiles, 2019Co-Authors: Ayako Yoshida, Minoru Yoshida, Tomohisa Kuzuyama, Makoto Nishiyama, Saori KosonoAbstract:Protein lysine N ^ε-Acetylation is one of the important factors regulating cellular metabolism. We performed a proteomic analysis to identify acetylated Proteins in the extremely thermophilic bacterium, Thermus thermophilus HB27. A total of 335 unique acetylated lysine residues, including many metabolic enzymes and ribosomal Proteins, were identified in 208 Proteins. Enzymes involved in amino acid metabolism were the most abundant among acetylated metabolic Proteins. 2-Isopropylmalate synthase (IPMS), which catalyzes the first step in leucine biosynthesis, was acetylated at four lysine residues. Acetylation-mimicking mutations at Lys332 markedly decreased IPMS activity in vitro, suggesting that Lys332, which is located in subdomain II, plays a regulatory role in IPMS activity. We also investigated the Acetylation-deAcetylation mechanism of IPMS and revealed that it was acetylated non-enzymatically by acetyl-CoA and deacetylated enzymatically by TT_C0104. The present results suggest that leucine biosynthesis is regulated by post-translational Protein modifications, in addition to feedback inhibition/repression, and that metabolic enzymes are regulated by Protein Acetylation in T. thermophilus .
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Protein Acetylation on 2-isopropylmalate synthase from Thermus thermophilus HB27.
Extremophiles : life under extreme conditions, 2019Co-Authors: Ayako Yoshida, Minoru Yoshida, Tomohisa Kuzuyama, Makoto Nishiyama, Saori KosonoAbstract:Protein lysine Ne-Acetylation is one of the important factors regulating cellular metabolism. We performed a proteomic analysis to identify acetylated Proteins in the extremely thermophilic bacterium, Thermus thermophilus HB27. A total of 335 unique acetylated lysine residues, including many metabolic enzymes and ribosomal Proteins, were identified in 208 Proteins. Enzymes involved in amino acid metabolism were the most abundant among acetylated metabolic Proteins. 2-Isopropylmalate synthase (IPMS), which catalyzes the first step in leucine biosynthesis, was acetylated at four lysine residues. Acetylation-mimicking mutations at Lys332 markedly decreased IPMS activity in vitro, suggesting that Lys332, which is located in subdomain II, plays a regulatory role in IPMS activity. We also investigated the Acetylation-deAcetylation mechanism of IPMS and revealed that it was acetylated non-enzymatically by acetyl-CoA and deacetylated enzymatically by TT_C0104. The present results suggest that leucine biosynthesis is regulated by post-translational Protein modifications, in addition to feedback inhibition/repression, and that metabolic enzymes are regulated by Protein Acetylation in T. thermophilus.
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Protein Acetylation involved in streptomycin biosynthesis in Streptomyces griseus.
Journal of proteomics, 2016Co-Authors: Yuji Ishigaki, Genki Akanuma, Minoru Yoshida, Sueharu Horinouchi, Saori Kosono, Yasuo OhnishiAbstract:Abstract Protein Acetylation, the reversible addition of an acetyl group to lysine residues, is a Protein post-translational modification ubiquitous in living cells. Although the involvement of Protein Acetylation in the regulation of primary metabolism has been revealed, the function of Protein Acetylation is largely unknown in secondary metabolism. Here, we characterized Protein Acetylation in Streptomyces griseus , a streptomycin producer. Protein Acetylation was induced in the stationary and sporulation phases in liquid and solid cultures, respectively, in S. griseus . By comprehensive acetylome analysis, we identified 134 acetylated Proteins with 162 specific acetylated sites. Acetylation was found in Proteins related to primary metabolism and translation, as in other bacteria. However, StrM, a deoxysugar epimerase involved in streptomycin biosynthesis, was identified as a highly acetylated Protein by 2-DE-based proteomic analysis. The Lys70 residue, which is critical for the enzymatic activity of StrM, was the major Acetylation site. Thus, Acetylation of Lys70 was presumed to abolish enzymatic activity of StrM. In accordance with this notion, an S. griseus mutant producing the Acetylation-mimic K70Q StrM hardly produced streptomycin, though the K70Q mutation apparently decreased the stability of StrM. A putative lysine acetyltransferase (KAT) SGR1683 in S. griseus , as well as the Escherichia coli KAT YfiQ, acetylated Lys70 of StrM in vitro . Furthermore, absolute quantification analysis estimated that 13% of StrM molecules were acetylated in mycelium grown in solid culture for 3 days. These results indicate that StrM Acetylation is of biological significance. We propose that StrM Acetylation functions as a limiter of streptomycin biosynthesis in S. griseus . Biological significance Protein Acetylation has been extensively studied not only in eukaryotes, but also in prokaryotes. The acetylome has been analyzed in more than 14 bacterial species. Here, by comprehensive acetylome analysis, we showed that Acetylation was found in Proteins related to primary metabolism and translation in Streptomyces griseus , similarly to other bacteria. However, five Proteins involved in secondary metabolism were also identified as acetylated Proteins; these Proteins are enzymes in the biosynthesis of streptomycin (StrB1 and StrS), grixazone (GriF), a nonribosomal peptide (NRPS1–2), and a siderophore (AlcC). Additionally, StrM in streptomycin biosynthesis was identified as a highly acetylated Protein by 2-DE-based proteomic analysis; approximately 13% of StrM molecules were acetylated. The Acetylation occurs at Lys70 to abolish the enzymatic activity of StrM, suggesting that StrM Acetylation functions as a limiter of streptomycin biosynthesis in S. griseus . This is the first detailed analysis of Protein Acetylation of an enzyme involved in secondary metabolism.
