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Tsuneyuki Tatsuke - One of the best experts on this subject based on the ideXlab platform.
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Gene Structure and cDNA sequence of 2-Cys peroxiredoxin in the harmful algal bloom species Chattonella marina and its Gene transcription under different light intensities
European Journal of Phycology, 2017Co-Authors: Koki Mukai, Yohei Shimasaki, Ayano Teramoto, Xuchun Qiu, Yoko Kato-unoki, Jae Man Lee, Naohiro Mizoguchi, Mst Ruhina Margia Khanam, Hina Satone, Tsuneyuki TatsukeAbstract:ABSTRACTWe investigated the Gene Structure and predicted amino acid sequence of the antioxidant enzyme 2-Cys peroxiredoxin (2-Cys Prx) in the raphidophyte Chattonella marina, which is a harmful algal bloom (HAB) species. The open reading frame of 2-Cys Prx was 585 bp long and encoded a protein consisting of 195 amino acids. The putative amino acid sequence contained two cysteine residues located at the 49th and 170th amino acid positions from the N-terminal methionine residue. The sequence also possessed 2-Cys Prx characteristic motifs, F (FFYPLDFTFVCPTEI) and EVCP. The position of the 2-Cys Prx Gene relative to several others (ycf59 – 2-CysPrx – rpl35 – rpl20) was the same as that found in the chloroplast genome in the raphidophyte Heterosigma akashiwo. Upstream of the 2-Cys Prx Gene, possible TATA and GGA motifs recognized by nuclear-encoded plastid RNA polymerase (NEP), and a possible -10 box and -35 box recognized by plastid-encoded plastid RNA polymerase (PEP) were observed. We measured the transcrip...
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Gene Structure and cDNA sequence of 2-Cys peroxiredoxin in the harmful algal bloom species Chattonella marina and its Gene transcription under different light intensities
2017Co-Authors: Koki Mukai, Yohei Shimasaki, Ayano Teramoto, Xuchun Qiu, Yoko Kato-unoki, Jae Man Lee, Naohiro Mizoguchi, Mst Ruhina Margia Khanam, Hina Satone, Tsuneyuki TatsukeAbstract:We investigated the Gene Structure and predicted amino acid sequence of the antioxidant enzyme 2-Cys peroxiredoxin (2-Cys Prx) in the raphidophyte Chattonella marina, which is a harmful algal bloom (HAB) species. The open reading frame of 2-Cys Prx was 585 bp long and encoded a protein consisting of 195 amino acids. The putative amino acid sequence contained two cysteine residues located at the 49th and 170th amino acid positions from the N-terminal methionine residue. The sequence also possessed 2-Cys Prx characteristic motifs, F (FFYPLDFTFVCPTEI) and EVCP. The position of the 2-Cys Prx Gene relative to several others (ycf59 – 2-CysPrx – rpl35 – rpl20) was the same as that found in the chloroplast genome in the raphidophyte Heterosigma akashiwo. Upstream of the 2-Cys Prx Gene, possible TATA and GGA motifs recognized by nuclear-encoded plastid RNA polymerase (NEP), and a possible -10 box and -35 box recognized by plastid-encoded plastid RNA polymerase (PEP) were observed. We measured the transcript levels of 2-Cys Prx in C. marina cells grown under three different light intensities (0, 100, 1000 µmol photons m–2 s–1, 14-h light/8-h dark photoperiod) by quantitative PCR. The 2-Cys Prx transcript level in cells grown under the highest light intensity on day 3 was threefold that on day 0 but two lower light intensities resulted in relatively stable transcription levels. The 2-Cys Prx transcript level was significantly positively related to the H2O2 concentration per cell and the H2O2 scavenging activity per cell. These results suggest that C. marina 2-Cys Prx functions in the chloroplast and its transcription could be regulated by both NEP and PEP. Moreover, the 2-Cys Prx transcript level might increase to remove excessive H2O2 produced under strong light conditions in order to maintain cell proliferation activity.
Paul G. Fitzgerald - One of the best experts on this subject based on the ideXlab platform.
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Primary sequence, secondary Structure, Gene Structure, and assembly properties suggests that the lens-specific cytoskeletal protein filensin represents a novel class of intermediate filament protein.
Experimental eye research, 1998Co-Authors: John F Hess, Jodi T. Casselman, Allen Kong, Paul G. FitzgeraldAbstract:The ocular lens fiber cell assembles a novel cytoskeletal element, the Beaded Filament, from CP49 and filensin, two proteins expressed only in the differentiated lens fiber cell. We report the primary sequence, secondary structural analysis, Gene Structure and Yeast Two Hybrid interaction data for human filensin, and develop a consensus model of filensin from the human and previously reported bovine and chicken filensin sequences. This consensus model, combined with Gene Structure and Yeast Two Hybrid studies establish that filensin is a member of the Intermediate Filament family of proteins. Specifically, filensin exhibits (1) divergence at amino acid sequence motifs otherwise highly conserved among intermediate filament proteins, (2) a loss of 29 amino acids from the central rod domain which is unique among cytoplasmic intermediate filament proteins, (3) an absence of sequence identity with any existing class of intermediate filament protein, (4) a Gene Structure unique among intermediate filament family, (5) an inability to dimerize with representatives of Type I, II, and III intermediate filament proteins. Thus, at each level of analysis, we find that filensin is similar to the consensus model of intermediate filament proteins, supporting our conclusion that filensin's relatedness to the IF family is not the consequence of convergent evolution. However, filensin also shows unique or extreme distinctions from the consensus intermediate filament protein at each level of analysis, indicating that filensin constitutes a novel class of IF protein. Some of filensin's unique features are incompatible with current models of IF assembly. Analysis of filensin Gene Structure suggests that the 29 amino acid reduction in the central rod domain was not the result of a single splice site mutation, the mechanism suggested for the transition between nuclear lamins and cytoplasmic intermediate filament proteins.
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Gene Structure and cDNA sequence identify the beaded filament protein CP49 as a highly divergent type I intermediate filament protein.
The Journal of biological chemistry, 1996Co-Authors: John F Hess, Jodi T. Casselman, Paul G. FitzgeraldAbstract:Abstract The fiber cell of the vertebrate ocular lens assembles a cytoskeletal Structure, the beaded filament, which contains two proteins unique to the fiber cell: CP49 (phakinin) and CP115/CP95 (filensin). We report here the complete primary sequence and Gene Structure for human CP49. These data show that CP49 is a member of the intermediate filament family, but highly unusual in several regards. 1) CP49 primary sequence does not permit unambiguous assignment to any existing class of intermediate filament protein, but exhibits a Gene Structure that is identical to the Type I cytokeratins. 2) CP49 essentially lacks one of the three major domains that characterize all intermediate filament proteins, the carboxyl-terminal tail domain. 3) CP49 shows substitutions at 3 of 4 residues in the otherwise highly conserved intermediate filament protein motif LNDR. Notably, this divergence includes an Arg to Cys substitution that has only been observed in the mutant human cytokeratin K14, a mutation shown to cause the skin blistering seen in the Genetic disorder Dowling-Meara epidermolysis bullosa simplex.
Koki Mukai - One of the best experts on this subject based on the ideXlab platform.
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Gene Structure and cDNA sequence of 2-Cys peroxiredoxin in the harmful algal bloom species Chattonella marina and its Gene transcription under different light intensities
European Journal of Phycology, 2017Co-Authors: Koki Mukai, Yohei Shimasaki, Ayano Teramoto, Xuchun Qiu, Yoko Kato-unoki, Jae Man Lee, Naohiro Mizoguchi, Mst Ruhina Margia Khanam, Hina Satone, Tsuneyuki TatsukeAbstract:ABSTRACTWe investigated the Gene Structure and predicted amino acid sequence of the antioxidant enzyme 2-Cys peroxiredoxin (2-Cys Prx) in the raphidophyte Chattonella marina, which is a harmful algal bloom (HAB) species. The open reading frame of 2-Cys Prx was 585 bp long and encoded a protein consisting of 195 amino acids. The putative amino acid sequence contained two cysteine residues located at the 49th and 170th amino acid positions from the N-terminal methionine residue. The sequence also possessed 2-Cys Prx characteristic motifs, F (FFYPLDFTFVCPTEI) and EVCP. The position of the 2-Cys Prx Gene relative to several others (ycf59 – 2-CysPrx – rpl35 – rpl20) was the same as that found in the chloroplast genome in the raphidophyte Heterosigma akashiwo. Upstream of the 2-Cys Prx Gene, possible TATA and GGA motifs recognized by nuclear-encoded plastid RNA polymerase (NEP), and a possible -10 box and -35 box recognized by plastid-encoded plastid RNA polymerase (PEP) were observed. We measured the transcrip...
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Gene Structure and cDNA sequence of 2-Cys peroxiredoxin in the harmful algal bloom species Chattonella marina and its Gene transcription under different light intensities
2017Co-Authors: Koki Mukai, Yohei Shimasaki, Ayano Teramoto, Xuchun Qiu, Yoko Kato-unoki, Jae Man Lee, Naohiro Mizoguchi, Mst Ruhina Margia Khanam, Hina Satone, Tsuneyuki TatsukeAbstract:We investigated the Gene Structure and predicted amino acid sequence of the antioxidant enzyme 2-Cys peroxiredoxin (2-Cys Prx) in the raphidophyte Chattonella marina, which is a harmful algal bloom (HAB) species. The open reading frame of 2-Cys Prx was 585 bp long and encoded a protein consisting of 195 amino acids. The putative amino acid sequence contained two cysteine residues located at the 49th and 170th amino acid positions from the N-terminal methionine residue. The sequence also possessed 2-Cys Prx characteristic motifs, F (FFYPLDFTFVCPTEI) and EVCP. The position of the 2-Cys Prx Gene relative to several others (ycf59 – 2-CysPrx – rpl35 – rpl20) was the same as that found in the chloroplast genome in the raphidophyte Heterosigma akashiwo. Upstream of the 2-Cys Prx Gene, possible TATA and GGA motifs recognized by nuclear-encoded plastid RNA polymerase (NEP), and a possible -10 box and -35 box recognized by plastid-encoded plastid RNA polymerase (PEP) were observed. We measured the transcript levels of 2-Cys Prx in C. marina cells grown under three different light intensities (0, 100, 1000 µmol photons m–2 s–1, 14-h light/8-h dark photoperiod) by quantitative PCR. The 2-Cys Prx transcript level in cells grown under the highest light intensity on day 3 was threefold that on day 0 but two lower light intensities resulted in relatively stable transcription levels. The 2-Cys Prx transcript level was significantly positively related to the H2O2 concentration per cell and the H2O2 scavenging activity per cell. These results suggest that C. marina 2-Cys Prx functions in the chloroplast and its transcription could be regulated by both NEP and PEP. Moreover, the 2-Cys Prx transcript level might increase to remove excessive H2O2 produced under strong light conditions in order to maintain cell proliferation activity.
John F Hess - One of the best experts on this subject based on the ideXlab platform.
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Primary sequence, secondary Structure, Gene Structure, and assembly properties suggests that the lens-specific cytoskeletal protein filensin represents a novel class of intermediate filament protein.
Experimental eye research, 1998Co-Authors: John F Hess, Jodi T. Casselman, Allen Kong, Paul G. FitzgeraldAbstract:The ocular lens fiber cell assembles a novel cytoskeletal element, the Beaded Filament, from CP49 and filensin, two proteins expressed only in the differentiated lens fiber cell. We report the primary sequence, secondary structural analysis, Gene Structure and Yeast Two Hybrid interaction data for human filensin, and develop a consensus model of filensin from the human and previously reported bovine and chicken filensin sequences. This consensus model, combined with Gene Structure and Yeast Two Hybrid studies establish that filensin is a member of the Intermediate Filament family of proteins. Specifically, filensin exhibits (1) divergence at amino acid sequence motifs otherwise highly conserved among intermediate filament proteins, (2) a loss of 29 amino acids from the central rod domain which is unique among cytoplasmic intermediate filament proteins, (3) an absence of sequence identity with any existing class of intermediate filament protein, (4) a Gene Structure unique among intermediate filament family, (5) an inability to dimerize with representatives of Type I, II, and III intermediate filament proteins. Thus, at each level of analysis, we find that filensin is similar to the consensus model of intermediate filament proteins, supporting our conclusion that filensin's relatedness to the IF family is not the consequence of convergent evolution. However, filensin also shows unique or extreme distinctions from the consensus intermediate filament protein at each level of analysis, indicating that filensin constitutes a novel class of IF protein. Some of filensin's unique features are incompatible with current models of IF assembly. Analysis of filensin Gene Structure suggests that the 29 amino acid reduction in the central rod domain was not the result of a single splice site mutation, the mechanism suggested for the transition between nuclear lamins and cytoplasmic intermediate filament proteins.
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Gene Structure and cDNA sequence identify the beaded filament protein CP49 as a highly divergent type I intermediate filament protein.
The Journal of biological chemistry, 1996Co-Authors: John F Hess, Jodi T. Casselman, Paul G. FitzgeraldAbstract:Abstract The fiber cell of the vertebrate ocular lens assembles a cytoskeletal Structure, the beaded filament, which contains two proteins unique to the fiber cell: CP49 (phakinin) and CP115/CP95 (filensin). We report here the complete primary sequence and Gene Structure for human CP49. These data show that CP49 is a member of the intermediate filament family, but highly unusual in several regards. 1) CP49 primary sequence does not permit unambiguous assignment to any existing class of intermediate filament protein, but exhibits a Gene Structure that is identical to the Type I cytokeratins. 2) CP49 essentially lacks one of the three major domains that characterize all intermediate filament proteins, the carboxyl-terminal tail domain. 3) CP49 shows substitutions at 3 of 4 residues in the otherwise highly conserved intermediate filament protein motif LNDR. Notably, this divergence includes an Arg to Cys substitution that has only been observed in the mutant human cytokeratin K14, a mutation shown to cause the skin blistering seen in the Genetic disorder Dowling-Meara epidermolysis bullosa simplex.
Mst Ruhina Margia Khanam - One of the best experts on this subject based on the ideXlab platform.
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Gene Structure and cDNA sequence of 2-Cys peroxiredoxin in the harmful algal bloom species Chattonella marina and its Gene transcription under different light intensities
European Journal of Phycology, 2017Co-Authors: Koki Mukai, Yohei Shimasaki, Ayano Teramoto, Xuchun Qiu, Yoko Kato-unoki, Jae Man Lee, Naohiro Mizoguchi, Mst Ruhina Margia Khanam, Hina Satone, Tsuneyuki TatsukeAbstract:ABSTRACTWe investigated the Gene Structure and predicted amino acid sequence of the antioxidant enzyme 2-Cys peroxiredoxin (2-Cys Prx) in the raphidophyte Chattonella marina, which is a harmful algal bloom (HAB) species. The open reading frame of 2-Cys Prx was 585 bp long and encoded a protein consisting of 195 amino acids. The putative amino acid sequence contained two cysteine residues located at the 49th and 170th amino acid positions from the N-terminal methionine residue. The sequence also possessed 2-Cys Prx characteristic motifs, F (FFYPLDFTFVCPTEI) and EVCP. The position of the 2-Cys Prx Gene relative to several others (ycf59 – 2-CysPrx – rpl35 – rpl20) was the same as that found in the chloroplast genome in the raphidophyte Heterosigma akashiwo. Upstream of the 2-Cys Prx Gene, possible TATA and GGA motifs recognized by nuclear-encoded plastid RNA polymerase (NEP), and a possible -10 box and -35 box recognized by plastid-encoded plastid RNA polymerase (PEP) were observed. We measured the transcrip...
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Gene Structure and cDNA sequence of 2-Cys peroxiredoxin in the harmful algal bloom species Chattonella marina and its Gene transcription under different light intensities
2017Co-Authors: Koki Mukai, Yohei Shimasaki, Ayano Teramoto, Xuchun Qiu, Yoko Kato-unoki, Jae Man Lee, Naohiro Mizoguchi, Mst Ruhina Margia Khanam, Hina Satone, Tsuneyuki TatsukeAbstract:We investigated the Gene Structure and predicted amino acid sequence of the antioxidant enzyme 2-Cys peroxiredoxin (2-Cys Prx) in the raphidophyte Chattonella marina, which is a harmful algal bloom (HAB) species. The open reading frame of 2-Cys Prx was 585 bp long and encoded a protein consisting of 195 amino acids. The putative amino acid sequence contained two cysteine residues located at the 49th and 170th amino acid positions from the N-terminal methionine residue. The sequence also possessed 2-Cys Prx characteristic motifs, F (FFYPLDFTFVCPTEI) and EVCP. The position of the 2-Cys Prx Gene relative to several others (ycf59 – 2-CysPrx – rpl35 – rpl20) was the same as that found in the chloroplast genome in the raphidophyte Heterosigma akashiwo. Upstream of the 2-Cys Prx Gene, possible TATA and GGA motifs recognized by nuclear-encoded plastid RNA polymerase (NEP), and a possible -10 box and -35 box recognized by plastid-encoded plastid RNA polymerase (PEP) were observed. We measured the transcript levels of 2-Cys Prx in C. marina cells grown under three different light intensities (0, 100, 1000 µmol photons m–2 s–1, 14-h light/8-h dark photoperiod) by quantitative PCR. The 2-Cys Prx transcript level in cells grown under the highest light intensity on day 3 was threefold that on day 0 but two lower light intensities resulted in relatively stable transcription levels. The 2-Cys Prx transcript level was significantly positively related to the H2O2 concentration per cell and the H2O2 scavenging activity per cell. These results suggest that C. marina 2-Cys Prx functions in the chloroplast and its transcription could be regulated by both NEP and PEP. Moreover, the 2-Cys Prx transcript level might increase to remove excessive H2O2 produced under strong light conditions in order to maintain cell proliferation activity.