Systematic Analysis of the Lysine Acetylome in <i>Vibrio parahemolyticus</i>

Lysine acetylation of proteins is a major post-translational modification that plays an important regulatory role in almost every aspect of cells, both eukaryotes and prokaryotes. Vibrio parahemolyticus, a model marine bacterium, is a worldwide cause of bacterial seafood-borne illness. Here, we conducted the first lysine acetylome in this bacterium through a combination of highly sensitive immune-affinity purification and high-resolution LC–MS/MS. Overall, we identified 1413 lysine acetylation sites in 656 proteins, which account for 13.6% of the total proteins in the cells; this is the highest ratio of acetyl proteins that has so far been identified in bacteria. The bioinformatics analysis of the acetylome showed that the acetylated proteins are involved in a wide range of cellular functions and exhibit diverse subcellular localizations. More specifically, proteins related to protein biosynthesis and carbon metabolism are the preferential targets of lysine acetylation. Moreover, two types of acetylation motifs, a lysine or arginine at the +4/+5 positions and a tyrosine, histidine, or phenylalanine at the +1/+2 positions, were revealed from the analysis of the acetylome. Additionally, protein interaction network analysis demonstrates that a wide range of interactions are modulated by protein acetylation. This study provides a significant beginning for the in-depth exploration of the physiological role of lysine acetylation in V. parahemolyticus

Systematic Analysis of the Lysine Acetylome in <i>Vibrio parahemolyticus</i>

Lysine acetylation of proteins is a major post-translational modification that plays an important regulatory role in almost every aspect of cells, both eukaryotes and prokaryotes. Vibrio parahemolyticus, a model marine bacterium, is a worldwide cause of bacterial seafood-borne illness. Here, we conducted the first lysine acetylome in this bacterium through a combination of highly sensitive immune-affinity purification and high-resolution LC–MS/MS. Overall, we identified 1413 lysine acetylation sites in 656 proteins, which account for 13.6% of the total proteins in the cells; this is the highest ratio of acetyl proteins that has so far been identified in bacteria. The bioinformatics analysis of the acetylome showed that the acetylated proteins are involved in a wide range of cellular functions and exhibit diverse subcellular localizations. More specifically, proteins related to protein biosynthesis and carbon metabolism are the preferential targets of lysine acetylation. Moreover, two types of acetylation motifs, a lysine or arginine at the +4/+5 positions and a tyrosine, histidine, or phenylalanine at the +1/+2 positions, were revealed from the analysis of the acetylome. Additionally, protein interaction network analysis demonstrates that a wide range of interactions are modulated by protein acetylation. This study provides a significant beginning for the in-depth exploration of the physiological role of lysine acetylation in V. parahemolyticus

Systematic Analysis of the Lysine Acetylome in <i>Vibrio parahemolyticus</i>

Lysine acetylation of proteins is a major post-translational modification that plays an important regulatory role in almost every aspect of cells, both eukaryotes and prokaryotes. Vibrio parahemolyticus, a model marine bacterium, is a worldwide cause of bacterial seafood-borne illness. Here, we conducted the first lysine acetylome in this bacterium through a combination of highly sensitive immune-affinity purification and high-resolution LC–MS/MS. Overall, we identified 1413 lysine acetylation sites in 656 proteins, which account for 13.6% of the total proteins in the cells; this is the highest ratio of acetyl proteins that has so far been identified in bacteria. The bioinformatics analysis of the acetylome showed that the acetylated proteins are involved in a wide range of cellular functions and exhibit diverse subcellular localizations. More specifically, proteins related to protein biosynthesis and carbon metabolism are the preferential targets of lysine acetylation. Moreover, two types of acetylation motifs, a lysine or arginine at the +4/+5 positions and a tyrosine, histidine, or phenylalanine at the +1/+2 positions, were revealed from the analysis of the acetylome. Additionally, protein interaction network analysis demonstrates that a wide range of interactions are modulated by protein acetylation. This study provides a significant beginning for the in-depth exploration of the physiological role of lysine acetylation in V. parahemolyticus

Systematic Analysis of the Lysine Acetylome in <i>Vibrio parahemolyticus</i>

Lysine acetylation of proteins is a major post-translational modification that plays an important regulatory role in almost every aspect of cells, both eukaryotes and prokaryotes. Vibrio parahemolyticus, a model marine bacterium, is a worldwide cause of bacterial seafood-borne illness. Here, we conducted the first lysine acetylome in this bacterium through a combination of highly sensitive immune-affinity purification and high-resolution LC–MS/MS. Overall, we identified 1413 lysine acetylation sites in 656 proteins, which account for 13.6% of the total proteins in the cells; this is the highest ratio of acetyl proteins that has so far been identified in bacteria. The bioinformatics analysis of the acetylome showed that the acetylated proteins are involved in a wide range of cellular functions and exhibit diverse subcellular localizations. More specifically, proteins related to protein biosynthesis and carbon metabolism are the preferential targets of lysine acetylation. Moreover, two types of acetylation motifs, a lysine or arginine at the +4/+5 positions and a tyrosine, histidine, or phenylalanine at the +1/+2 positions, were revealed from the analysis of the acetylome. Additionally, protein interaction network analysis demonstrates that a wide range of interactions are modulated by protein acetylation. This study provides a significant beginning for the in-depth exploration of the physiological role of lysine acetylation in V. parahemolyticus

X‑ray Crystallographic Characterization of New Soluble Endohedral Fullerenes Utilizing the Popular C₈₂ Bucky Cage. Isolation and Structural Characterization of Sm@<i>C</i>_3<i>v</i>(7)‑C₈₂, Sm@<i>C</i>_<i>s</i>(6)‑C₈₂, and Sm@<i>C</i>₂(5)‑C₈₂

Three isomers of Sm@C₈₂ that are soluble in organic solvents were obtained from the carbon soot produced by vaporization of hollow carbon rods doped with Sm₂O₃/graphite powder in an electric arc. These isomers were numbered as Sm@C₈₂(I), Sm@C₈₂(II), and Sm@C₈₂(III) in order of their elution times from HPLC chromatography on a Buckyprep column with toluene as the eluent. The identities of isomers, Sm@C₈₂(I) as Sm@<i>C</i>_<i>s</i>(6)-C₈₂, Sm@C₈₂(II) as Sm@<i>C</i>_3<i>v</i>(7)-C₈₂, and Sm@C₈₂(III) as Sm@<i>C</i>₂(5)-C₈₂, were determined by single-crystal X-ray diffraction on cocrystals formed with Ni­(octaethylporphyrin). For endohedral fullerenes like La@C₈₂, which have three electrons transferred to the cage to produce the M³⁺@(C₈₂)^3– electronic distribution, generally only two soluble isomers (<i>e.g.</i>, La<i>@C</i>_2<i>v</i>(9)-C₈₂ (major) and La@<i>C</i>_<i>s</i>(6)-C₈₂ (minor)) are observed. In contrast, with samarium, which generates the M²⁺@(C₈₂)^2– electronic distribution, five soluble isomers of Sm@C₈₂ have been detected, three in this study, the other two in two related prior studies. The structures of the four Sm@C₈₂ isomers that are currently established are Sm@<i>C</i>₂(5)-C₈₂, Sm@<i>C</i>_<i>s</i>(6)-C₈₂, Sm@<i>C</i>_3<i>v</i>(7)-C₈₂, and Sm@<i>C</i>_2<i>v</i>(9)-C₈₂. All of these isomers obey the isolated pentagon rule (IPR) and are sequentially interconvertable through Stone–Wales transformations

X‑ray Crystallographic Characterization of New Soluble Endohedral Fullerenes Utilizing the Popular C₈₂ Bucky Cage. Isolation and Structural Characterization of Sm@<i>C</i>_3<i>v</i>(7)‑C₈₂, Sm@<i>C</i>_<i>s</i>(6)‑C₈₂, and Sm@<i>C</i>₂(5)‑C₈₂

Three isomers of Sm@C₈₂ that are soluble in organic solvents were obtained from the carbon soot produced by vaporization of hollow carbon rods doped with Sm₂O₃/graphite powder in an electric arc. These isomers were numbered as Sm@C₈₂(I), Sm@C₈₂(II), and Sm@C₈₂(III) in order of their elution times from HPLC chromatography on a Buckyprep column with toluene as the eluent. The identities of isomers, Sm@C₈₂(I) as Sm@<i>C</i>_<i>s</i>(6)-C₈₂, Sm@C₈₂(II) as Sm@<i>C</i>_3<i>v</i>(7)-C₈₂, and Sm@C₈₂(III) as Sm@<i>C</i>₂(5)-C₈₂, were determined by single-crystal X-ray diffraction on cocrystals formed with Ni­(octaethylporphyrin). For endohedral fullerenes like La@C₈₂, which have three electrons transferred to the cage to produce the M³⁺@(C₈₂)^3– electronic distribution, generally only two soluble isomers (<i>e.g.</i>, La<i>@C</i>_2<i>v</i>(9)-C₈₂ (major) and La@<i>C</i>_<i>s</i>(6)-C₈₂ (minor)) are observed. In contrast, with samarium, which generates the M²⁺@(C₈₂)^2– electronic distribution, five soluble isomers of Sm@C₈₂ have been detected, three in this study, the other two in two related prior studies. The structures of the four Sm@C₈₂ isomers that are currently established are Sm@<i>C</i>₂(5)-C₈₂, Sm@<i>C</i>_<i>s</i>(6)-C₈₂, Sm@<i>C</i>_3<i>v</i>(7)-C₈₂, and Sm@<i>C</i>_2<i>v</i>(9)-C₈₂. All of these isomers obey the isolated pentagon rule (IPR) and are sequentially interconvertable through Stone–Wales transformations

X‑ray Crystallographic Characterization of New Soluble Endohedral Fullerenes Utilizing the Popular C₈₂ Bucky Cage. Isolation and Structural Characterization of Sm@<i>C</i>_3<i>v</i>(7)‑C₈₂, Sm@<i>C</i>_<i>s</i>(6)‑C₈₂, and Sm@<i>C</i>₂(5)‑C₈₂

Three isomers of Sm@C₈₂ that are soluble in organic solvents were obtained from the carbon soot produced by vaporization of hollow carbon rods doped with Sm₂O₃/graphite powder in an electric arc. These isomers were numbered as Sm@C₈₂(I), Sm@C₈₂(II), and Sm@C₈₂(III) in order of their elution times from HPLC chromatography on a Buckyprep column with toluene as the eluent. The identities of isomers, Sm@C₈₂(I) as Sm@<i>C</i>_<i>s</i>(6)-C₈₂, Sm@C₈₂(II) as Sm@<i>C</i>_3<i>v</i>(7)-C₈₂, and Sm@C₈₂(III) as Sm@<i>C</i>₂(5)-C₈₂, were determined by single-crystal X-ray diffraction on cocrystals formed with Ni­(octaethylporphyrin). For endohedral fullerenes like La@C₈₂, which have three electrons transferred to the cage to produce the M³⁺@(C₈₂)^3– electronic distribution, generally only two soluble isomers (<i>e.g.</i>, La<i>@C</i>_2<i>v</i>(9)-C₈₂ (major) and La@<i>C</i>_<i>s</i>(6)-C₈₂ (minor)) are observed. In contrast, with samarium, which generates the M²⁺@(C₈₂)^2– electronic distribution, five soluble isomers of Sm@C₈₂ have been detected, three in this study, the other two in two related prior studies. The structures of the four Sm@C₈₂ isomers that are currently established are Sm@<i>C</i>₂(5)-C₈₂, Sm@<i>C</i>_<i>s</i>(6)-C₈₂, Sm@<i>C</i>_3<i>v</i>(7)-C₈₂, and Sm@<i>C</i>_2<i>v</i>(9)-C₈₂. All of these isomers obey the isolated pentagon rule (IPR) and are sequentially interconvertable through Stone–Wales transformations