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acetamido-fluorescein-glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n-Glu-S-acetamido-fluorescein-Cys-Gly
-
-
-
-
?
benzyl-glutathione + [Glu(-Cys)]n Gly
Gly + [Glu(-Cys)]n-Glu-S-benzyl-Cys-Gly
-
-
-
-
?
bimane-glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n-Glu-S-bimane-Cys-Gly
Cd2+-bis-glutathionate + [Glu(-Cys)]n-Gly
?
-
-
-
?
glutathione + Glu-Cys-Gly
Gly + [Glu(-Cys)]2-Gly
-
-
-
?
glutathione + [Glu(-Cys)]2-Gly
Gly + [Glu(-Cys)]3-Gly
-
-
-
?
glutathione + [Glu(-Cys)]3-Gly
Gly + [Glu(-Cys)]4-Gly
-
-
-
?
glutathione + [Glu(-Cys)]n -Gly
Gly + [Glu(-Cys)]n+1 -Gly
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
metal-bis-glutathionate + [Glu(-Cys)]n-Gly
?
Zn2+-bis-glutathionate is the best cosubstrate. The order of preference for the Me-GS2 substrate is Zn2+ > Cd2+ > Mn2+ > As5+ > As3+ > Cu2+ > Ag+
-
-
?
monobromobimane-glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n-Glu-S-monobromobimane-Cys-Gly
-
-
-
-
?
monochlorobimane + ?
?
-
-
-
-
?
nitrobenzyl-glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n-Glu-S-nitrobenzyl-Cys-Gly
-
-
-
-
?
S-butylglutathione + [Glu(-Cys)]n Gly
Gly + [Glu(-Cys)]n-Glu-S-butyl-Cys-Gly
-
-
-
-
?
S-ethylglutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n-Glu-S-ethyl-Cys-Gly
-
-
-
-
?
S-hexylglutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n-Glu-S-hexyl-Cys-Gly
-
-
-
-
?
S-methylglutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n-Glu-S-methyl-Cys-Gly
-
n = 2,3
-
-
?
S-propylglutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n-Glu-S-propyl-Cys-Gly
-
-
-
-
?
uracil-glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n-Glu-S-uracil-Cys-Gly
Zn2+-bis-glutathionate + [Glu(-Cys)]n-Gly
?
Zn2+-bis-glutathionate is the best cosubstrate
-
-
?
additional information
?
-
bimane-glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n-Glu-S-bimane-Cys-Gly
-
-
-
-
?
bimane-glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n-Glu-S-bimane-Cys-Gly
-
-
-
-
?
bimane-glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n-Glu-S-bimane-Cys-Gly
-
-
-
-
?
bimane-glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n-Glu-S-bimane-Cys-Gly
-
-
-
-
?
glutathione + [Glu(-Cys)]n -Gly
Gly + [Glu(-Cys)]n+1 -Gly
-
-
-
-
?
glutathione + [Glu(-Cys)]n -Gly
Gly + [Glu(-Cys)]n+1 -Gly
-
-
-
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
-
-
-
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
-
-
-
-
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
-
-
-
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
-
-
-
-
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
-
-
-
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
-
-
-
-
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
-
-
-
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
-
-
-
-
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
-
-
-
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
-
-
-
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
-
-
n = 2-11
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
-
n = 2-11
-
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
-
cellular functions are formation of heavy-metal binding peptides and degradation of glutathione-S-conjugates
-
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
-
synthesis of photochelatin
-
-
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
-
-
-
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
-
-
n = 2-11
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
-
n = 2-11
-
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
-
cellular functions are formation of heavy-metal binding peptides and degradation of glutathione-S-conjugates
-
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
-
-
-
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
-
-
-
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
-
-
-
-
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
-
-
-
-
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
G5ECE4
critical for heavy metal tolerance
-
-
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
G5ECE4
critical for heavy metal tolerance
-
-
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
-
-
-
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
-
-
-
-
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
-
-
-
-
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
-
-
-
-
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
-
-
-
-
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
-
-
-
-
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
-
-
-
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
-
-
-
-
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
-
-
-
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
-
-
-
-
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
-
-
-
-
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
-
-
-
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
-
-
-
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
-
-
-
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
-
-
-
-
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
-
-
n = 2-5
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
-
n = 2-5
-
-
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
-
-
-
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
-
-
-
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
-
-
-
-
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
Saccharomyces pombe
-
-
-
-
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
-
-
-
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
-
-
-
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
-
-
-
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
-
critical for heavy metal tolerance
-
-
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
-
-
-
?
glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n+1-Gly
-
-
-
-
?
uracil-glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n-Glu-S-uracil-Cys-Gly
-
-
-
-
?
uracil-glutathione + [Glu(-Cys)]n-Gly
Gly + [Glu(-Cys)]n-Glu-S-uracil-Cys-Gly
-
-
-
-
?
additional information
?
-
-
the presence of VdCl2 activates phytochelatin synthase and induces the synthesis of substantial amounts of phytochelatins
-
-
?
additional information
?
-
the PCS enzyme catalyzes transformation of GSH to give phytochelatins (PCs), it can effectively capture and enrich Cd2+ so that the generation and subsequent application process of CdS NPs is greatly improved
-
-
-
additional information
?
-
-
the PCS enzyme catalyzes transformation of GSH to give phytochelatins (PCs), it can effectively capture and enrich Cd2+ so that the generation and subsequent application process of CdS NPs is greatly improved
-
-
-
additional information
?
-
PC2 is the main polymerization product of PCS1, followed by PC3, low amount of PC4 formation. PCS1 has the highest activity of the three isozymes, PCS3 the lowest
-
-
-
additional information
?
-
PC2 is the main polymerization product of PCS1, followed by PC3, low amount of PC4 formation. PCS1 has the highest activity of the three isozymes, PCS3 the lowest
-
-
-
additional information
?
-
PC2 is the main polymerization product of PCS1, followed by PC3, low amount of PC4 formation. PCS1 has the highest activity of the three isozymes, PCS3 the lowest
-
-
-
additional information
?
-
-
PC2 is the main polymerization product of PCS1, followed by PC3, low amount of PC4 formation. PCS1 has the highest activity of the three isozymes, PCS3 the lowest
-
-
-
additional information
?
-
PC2 is the main polymerization product of PCS2, followed by PC3, low amount of PC4 formation. PCS1 has the highest activity of the three isozymes, PCS3 the lowest
-
-
-
additional information
?
-
PC2 is the main polymerization product of PCS2, followed by PC3, low amount of PC4 formation. PCS1 has the highest activity of the three isozymes, PCS3 the lowest
-
-
-
additional information
?
-
PC2 is the main polymerization product of PCS2, followed by PC3, low amount of PC4 formation. PCS1 has the highest activity of the three isozymes, PCS3 the lowest
-
-
-
additional information
?
-
-
PC2 is the main polymerization product of PCS2, followed by PC3, low amount of PC4 formation. PCS1 has the highest activity of the three isozymes, PCS3 the lowest
-
-
-
additional information
?
-
PC2 is the main polymerization product of PCS3, followed by PC3, low amount of PC4 formation. PCS1 has the highest activity of the three isozymes, PCS3 the lowest
-
-
-
additional information
?
-
PC2 is the main polymerization product of PCS3, followed by PC3, low amount of PC4 formation. PCS1 has the highest activity of the three isozymes, PCS3 the lowest
-
-
-
additional information
?
-
PC2 is the main polymerization product of PCS3, followed by PC3, low amount of PC4 formation. PCS1 has the highest activity of the three isozymes, PCS3 the lowest
-
-
-
additional information
?
-
-
PC2 is the main polymerization product of PCS3, followed by PC3, low amount of PC4 formation. PCS1 has the highest activity of the three isozymes, PCS3 the lowest
-
-
-
additional information
?
-
-
despite constitutive expression of the enzyme during most stages of plant development, Brassica juncea may react to prolonged exposure to Cd2+ with an increase of phytochelatin synthase protein in leaves
-
-
?
additional information
?
-
the enzyme does not use gamma-glutamylcysteine or phytochelatin2 as substrate
-
-
?
additional information
?
-
-
the enzyme does not use gamma-glutamylcysteine or phytochelatin2 as substrate
-
-
?
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metabolism
contrasting effects of enzyme mutation on As and Cd distribution to grains suggest the existence of at least partially distinct PC-dependent pathways for As and Cd
additional information
-
the cosmopolitan moss Leptodictyum riparium (Bryophyta) can accumulate, and seemingly tolerate, very high concentrations of toxic metals, including Cd. Leptodictyum riparium performs little Cd immobilization at the cell wall level, and therefore the metal enters the cytosol rather easily
evolution
evolution and functional differentiation of the recently diverged three phytochelatin synthase genes from Arundo donax, phylogenetic analysis and evolutionary modeling, overview. AdPCS1-3 proteins are significantly less divergent than other duplicated PCSs, displaying only 25-29 substitutions. All the canonical features of PCSs are present, namely the catalytic triad Cys56, His162, and Asp180. The lengths of both N- and C-terminal domains are comparable to those of previously validated PCSs. AdPCS1-3 genes evolved at different evolutionary rates
evolution
-
genes encoding phytochelatin synthases have been found in all vascular plants as well as some algae, fungi, diatoms and invertebrates. Horizontal gene transfer of phytochelatin synthases from bacteria to extremophilic green algae. A detailed phylogenetic analysis gives insight into the complicated evolutionary history of PCS genes and provides evidence for multiple horizontal gene transfer events from bacteria to eukaryotes within the gene family. A separate subgroup containing PCS-like genes within the PCS gene family is not supported since the PCS genes are monophyletic only when the PCS-like genes are included. Genotyping, overview
evolution
-
genes encoding phytochelatin synthases have been found in all vascular plants as well as some algae, fungi, diatoms and invertebrates. Horizontal gene transfer of phytochelatin synthases from bacteria to extremophilic green algae. A detailed phylogenetic analysis gives insight into the complicated evolutionary history of PCS genes and provides evidence for multiple horizontal gene transfer events from bacteria to eukaryotes within the gene family. A separate subgroup containing PCS-like genes within the PCS gene family is not supported since the PCS genes are monophyletic only when the PCS-like genes are included. Genotyping, overview
evolution
the two CDSs of OsPCS1 and OsPCS2 show 72% sequence identity at the nucleotide level, whereas the two proteins share overall 62.1% amino acid sequence identity. Moreover, both the intron sizes and nucleotide sequences are found to be highly differing between OsPCS1 and OsPCS2. Alignment of the deduced OsPCS1 and OsPCS2 polypeptides indicate the presence of N-terminal Phytochelatin (pfam05023) domain with high sequence identity (80.7%) including the conserved catalytic triad of Cys (C), His (H) and Asp (D). On the other hand, the C-terminal Phytochelatin_C (pfam09328) domain show moderate identity (57.68%) between these two polypeptides
evolution
-
the two CDSs of OsPCS1 and OsPCS2 show 72% sequence identity at the nucleotide level, whereas the two proteins share overall 62.1% amino acid sequence identity. Moreover, both the intron sizes and nucleotide sequences are found to be highly differing between OsPCS1 and OsPCS2. Alignment of the deduced OsPCS1 and OsPCS2 polypeptides indicate the presence of N-terminal Phytochelatin (pfam05023) domain with high sequence identity (80.7%) including the conserved catalytic triad of Cys (C), His (H) and Asp (D). On the other hand, the C-terminal Phytochelatin_C (pfam09328) domain show moderate identity (57.68%) between these two polypeptides
-
evolution
-
genes encoding phytochelatin synthases have been found in all vascular plants as well as some algae, fungi, diatoms and invertebrates. Horizontal gene transfer of phytochelatin synthases from bacteria to extremophilic green algae. A detailed phylogenetic analysis gives insight into the complicated evolutionary history of PCS genes and provides evidence for multiple horizontal gene transfer events from bacteria to eukaryotes within the gene family. A separate subgroup containing PCS-like genes within the PCS gene family is not supported since the PCS genes are monophyletic only when the PCS-like genes are included. Genotyping, overview
-
evolution
-
genes encoding phytochelatin synthases have been found in all vascular plants as well as some algae, fungi, diatoms and invertebrates. Horizontal gene transfer of phytochelatin synthases from bacteria to extremophilic green algae. A detailed phylogenetic analysis gives insight into the complicated evolutionary history of PCS genes and provides evidence for multiple horizontal gene transfer events from bacteria to eukaryotes within the gene family. A separate subgroup containing PCS-like genes within the PCS gene family is not supported since the PCS genes are monophyletic only when the PCS-like genes are included. Genotyping, overview
-
malfunction
AtPCS2-overexpressing transgenic Arabidopsis thaliana and Nicotiana tabacum plants display increased seed germination rates and seedling growth under high salt stress. In addition, transgenic Arabidopsis subjected to salt stress exhibit enhanced proline accumulation and reduced Na+/K+ ratios compared to wild-type plants. Effects of salt stress on seed germination and root elongation of AtPCS2-overexpressing transgenic plants, phenotype, overview
malfunction
genetically engineered plants having their OsPCS1 expression silenced via RNA interference (OsPCS1 RNAi) show no significant difference phenotype compared to wild-type plants. Treatment with buthionine sulfoximine, an inhibitor of GSH biosynthesis, significantly decreases Cd and As tolerance of rice seedlings. Concentrations of thiol peptides in the roots of OsPCS RNAi plants grown under Cd stress, overview
malfunction
genetically engineered plants having their OsPCS2 expression silenced via RNA interference (OsPCS2 RNAi) contain less phytochelatins (PCs) and more glutathione (GSH), the substrate of PC synthesis by PCS, than wild-type plants. OsPCS2 RNAi plants are sensitive to As(III) stress, but Cd tolerance is little affected. Treatment with buthionine sulfoximine, an inhibitor of GSH biosynthesis, significantly decreases Cd and As tolerance of rice seedlings. Concentrations of thiol peptides in the roots of OsPCS RNAi plants grown under Cd stress, overview
malfunction
RNAi-mediated grain-specific silencing of OsPCS decreases cadmium accumulation in rice grain
malfunction
the As(III)-sensitive phenotype of cad1-3 seedlings is completely rescued by the introduction of OsPCS1full variant, whereas growth of the plants expressing the other OsPCS variants is inhibited by As(III) as strongly as that of cad1-3. Similarly, OsPCS1full introduction complements the Cd-sensitive phenotype of cad1-3, while the other OsPCS1 variants do not. OsPCS1 mutant plants show increased sensitivity to Cd and As(III) stress
malfunction
the As(III)-sensitive phenotype of cad1-3 seedlings is completely rescued by the introduction of OsPCS1full variant, whereas growth of the plants expressing the other OsPCS1 variants is inhibited by As(III) as strongly as that of cad1-3. Similarly, OsPCS1full introduction complements the Cd-sensitive phenotype of cad1-3, while the other OsPCS1 variants do not
malfunction
the As(III)-sensitive phenotype of cad1-3 seedlings is completely rescued by the introduction of OsPCS1full variant, whereas growth of the plants expressing the other OsPCS1 variants is inhibited by As(III) as strongly as that of cad1-3. Similarly, OsPCS1full introduction complements the Cd-sensitive phenotype of cad1-3, while the other OsPCS1 variants do not. OsPCS1 mutant plants show increased sensitivity to Cd and As(III) stress
malfunction
the As(III)-sensitive phenotype of cad1-3 seedlings is completely rescued by the introduction of OsPCS1full variant, whereas growth of the plants expressing the other OsPCS1 variants is inhibited by As(III) as strongly as that of cad1-3. Similarly, OsPCS1full introduction complements the Cd-sensitive phenotype of cad1-3, while the other OsPCS1 variants do not. OsPCS1 mutant plants show increased sensitivity to Cd and As(III) stress. Distribution of As and Cd is altered in shoot and grains of OsPCS1 mutants
malfunction
transgenic plants highly expressing OsPCS1 show significantly lower As levels in grains than do wild-type plants
malfunction
-
RNAi-mediated grain-specific silencing of OsPCS decreases cadmium accumulation in rice grain
-
malfunction
-
AtPCS2-overexpressing transgenic Arabidopsis thaliana and Nicotiana tabacum plants display increased seed germination rates and seedling growth under high salt stress. In addition, transgenic Arabidopsis subjected to salt stress exhibit enhanced proline accumulation and reduced Na+/K+ ratios compared to wild-type plants. Effects of salt stress on seed germination and root elongation of AtPCS2-overexpressing transgenic plants, phenotype, overview
-
physiological function
phytochelatins play an important role in detoxification of heavy metals in plants
physiological function
-
at CdSO4 concentrations up to 0.06 mM that have no or only slightly toxic effects on the growth of wild type Arabidopsis seedlings, phytochelatin synthase(PCS1) overexpression results in a decrease in Cd tolerance compared with the wild type, as mainly revealed by a reduced root growth. At higher Cd concentrations (0.09-0.18 mM CdSO4) toxic to wild type seedlings (as manifested by a significant decrease in fresh weight and root growth as well as by foliar chlorosis) PCS1 overexpression confers an increase in Cd tolerance
physiological function
enhanced metal (Cd2+ and As5+) accumulation is due to post-translational activation of the enzyme in the presence of Cd2+ ion
physiological function
-
enzyme expression leads to increased Cd2+ accumulation and enhanced metal tolerance. Enzyme overexpression leads to an increase in the antioxidative activity and a decrease in the oxidative damage induced by Cd toxicity
physiological function
the enzyme is involved in cellular cadmium tolerance
physiological function
the enzyme is involved in cellular cadmium tolerance
physiological function
-
the enzyme is involved in the response of Nelumbo nucifera to cadmium stress
physiological function
-
yeast cells producing both Arabidopsis thaliana phytochelatin synthase and cysteine desulfhydrase show a higher level of arsenic accumulation than a simple cumulative effect of expressing both enzymes confirming the importance of coordinated action of hydrogen sulfide and phytochelatins in the overall bioaccumulation of arsenic
physiological function
the enzyme binds, localizes, stores or sequesters heavy metals in plant cells
physiological function
the enzyme confers resistance on Cd2+ stress
physiological function
-
the enzyme has a major role in the detoxification of heavy metals. Escherichia coli with overexpressed phytochelatin synthase 1 has enhanced tolerance to cadmium, copper, sodium, and mercury
physiological function
-
analysis of the possible involvement of the enzyme in the homeostasis of metallic micronutrients, and its role in the detoxification of non-essential metals, such as Cd2+. Neither in vivo nor in vitro exposure to Zn results in PCS activation and significant phytochelatin (PC) biosynthesis, while Fe(II)/(III) and Cd2+ are able to activate enzyme PCS in vitro, as well as to induce PC accumulation in vivo. Function of enzyme PCS and phytochelatins in managing Fe homeostasis in the carophyte Nitella mucronata
physiological function
-
in plant cells, Cd ions are highly noxious even at low concentrations, with subsequent severe negative effects. Activation of phytochelatin synthase (PCS) and glutathione-S-transferase, but minimally phytochelatin synthesis, play a role to counteract Cd toxicity in Leptodictyum riparium, for minimizing the cellular damage caused by the metal. The highest Cd concentrations activates the formation of gamma-glutamyl-cysteinyl-bimane (GS-bimane) in the cytosol, possibly catalyzed by the peptidase activity of phytochelatin synthase. PCS activation is self-regulated, because its product poly(4-glutamyl-cysteinyl)glycine (PCn) chelates Cd, and the reaction stops when free Cd2+ ions are no longer available. Besides being a gamma-EC transpeptidase, PCS is also a cysteine peptidase that may regulate the cytosolic catabolism of gamma-glutamyl-cysteinyl (GS)-conjugates. In this case, GS-conjugates with MCB (GS-bimane) can be cleaved into gamma-gamma-glutamyl-cysteine and glycine, a reaction stimulated by some metals, particularly Cd, Zn, and Cu
physiological function
isozyme OsPCS2 is a major isozyme controlling phytochelatin (PC) synthesis, and PCs are important for As tolerance in rice. PC synthesis may make a smaller contribution to Cd tolerance in rice. Synthesis of thiol peptides in response to Cd or As(III) stress in rice roots
physiological function
phytochelatin synthase (PCS) is an enzyme involved in the synthesis of phytochelatins, cysteine-rich peptides which play a key role in heavy metal (HM) detoxification of plants. Mulberry has the potential to remediate HM-contaminated soils. The two PCS genes in Morus notabilis (PCS1 and 2) are involved in HM detoxification in Morus. MnPCS1 plays a more important role in Cd detoxification than MnPCS2. MnPCS enzymes can markedly increase the tolerance of the transgenic plants at high concentrations of Zn2+, while the corresponding relationship between Cd2+ accumulation and the expression of MnPCSs are not observed. There might be some factor-dependent posttranscriptional regulation of PCS, like intron-mediated enhancement, and/or an optimum PCS level for tolerance to and accumulation of HMs in plants
physiological function
phytochelatin synthase (PCS) is an enzyme involved in the synthesis of phytochelatins, cysteine-rich peptides which play a key role in heavy metal (HM) detoxification of plants. Mulberry has the potential to remediate HM-contaminated soils. The two PCS genes in Morus notabilis (PCS1 and 2) are involved in HM detoxification in Morus. MnPCS1 plays a more important role in Cd detoxification than MnPCS2. The enzymes can markedly increase the tolerance of the transgenic plants at high concentrations of Zn2+, while the corresponding relationship between Cd2+ accumulation and the expression of MnPCSs are not observed. There might be some factor-dependent posttranscriptional regulation of PCS, like intron-mediated enhancement, and/or an optimum PCS level for tolerance to and accumulation of HMs in plants
physiological function
phytochelatin synthase (PCS) is an enzyme that synthesizes phytochelatins, which are metal-binding peptides. It plays an important role in heavy metal detoxification or tolerance. Function of Arabidopsis thaliana phytochelatin synthase 2 (AtPCS2) in the salt stress response. AtPCS2 plays a positive role in seed germination and seedling growth under salt stress through a series of indirect effects that are likely involved in H2O2 scavenging, regulation of osmotic adjustment and ion homeostasis
physiological function
phytochelatin synthase has contrasting effects on cadmium and arsenic accumulation in rice grains
physiological function
phytochelatin synthase has contrasting effects on cadmium and arsenic accumulation in rice grains. Physiological role of Oryza sativa phytochelatin synthase 1 (OsPCS1) in the distribution and detoxification of arsenic (As) and cadmium (Cd), importance of OsPCS1-dependent PC synthesis for rice As(III) and Cd tolerance
physiological function
phytochelatin synthase has contrasting effects on cadmium and arsenic accumulation in rice grains. Physiological role of Oryza sativa phytochelatin synthase 1full (OsPCS1full) in the distribution and detoxification of arsenic (As) and cadmium (Cd), importance of OsPCS1-dependent PC synthesis for rice As(III) and Cd tolerance
physiological function
phytochelatin synthase OsPCS1 plays a crucial role in reducing arsenic levels in rice grains. Redundancy between OsPCS1 and OsPCS2
physiological function
phytochelatin synthases (PCSs) play pivotal roles in the detoxification of heavy metals and metalloids in plants
physiological function
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phytochelatins (PCs) mediate high-affinity binding and contribute to detoxification of heavy metal ions and metalloids, such as cadmium or arsenic, by promoting the vacuo-lysosomal sequestration of heavy metals. These compounds are enzymatically synthesized from reduced glutathione (GSH) and related thiols in a gamma-glutamylcysteinyltranspeptidation reaction catalyzed by phytochelatin synthase (PCS)
physiological function
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phytochelatins (PCs) mediate high-affinity binding and contribute to detoxification of heavy metal ions and metalloids, such as cadmium or arsenic, by promoting the vacuolysosomal sequestration of heavy metals. These compounds are enzymatically synthesized from reduced glutathione (GSH) and related thiols in a gamma-glutamylcysteinyltranspeptidation reaction catalyzed by phytochelatin synthase (PCS)
physiological function
pyhtochelatins (PCs) are important for As tolerance in rice. PC synthesis may make a smaller contribution to Cd tolerance in rice. Synthesis of thiol peptides in response to Cd or As(III) stress in rice roots
physiological function
redundancy between OsPCS1 and OsPCS2
physiological function
role of of enzyme PCS in abiotic stress tolerance
physiological function
the OsPCS2 exhibits root- and shoot-specific differential ratios of alternatively spliced transcripts in Oryza sativa subsp. indica rice under Cd stress, and plays role in Cd and As stress tolerance and accumulation
physiological function
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the OsPCS2 exhibits root- and shoot-specific differential ratios of alternatively spliced transcripts in Oryza sativa subsp. indica rice under Cd stress, and plays role in Cd and As stress tolerance and accumulation
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physiological function
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phytochelatin synthase (PCS) is an enzyme that synthesizes phytochelatins, which are metal-binding peptides. It plays an important role in heavy metal detoxification or tolerance. Function of Arabidopsis thaliana phytochelatin synthase 2 (AtPCS2) in the salt stress response. AtPCS2 plays a positive role in seed germination and seedling growth under salt stress through a series of indirect effects that are likely involved in H2O2 scavenging, regulation of osmotic adjustment and ion homeostasis
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physiological function
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phytochelatins (PCs) mediate high-affinity binding and contribute to detoxification of heavy metal ions and metalloids, such as cadmium or arsenic, by promoting the vacuo-lysosomal sequestration of heavy metals. These compounds are enzymatically synthesized from reduced glutathione (GSH) and related thiols in a gamma-glutamylcysteinyltranspeptidation reaction catalyzed by phytochelatin synthase (PCS)
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physiological function
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phytochelatins (PCs) mediate high-affinity binding and contribute to detoxification of heavy metal ions and metalloids, such as cadmium or arsenic, by promoting the vacuolysosomal sequestration of heavy metals. These compounds are enzymatically synthesized from reduced glutathione (GSH) and related thiols in a gamma-glutamylcysteinyltranspeptidation reaction catalyzed by phytochelatin synthase (PCS)
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A182G/A282V/G329S
the mutant has strongly reduced activity compared to the wild type enzyme. The mutant improves the Cd2+ tolerance of Arabidopsis thaliana
A59V
the mutant has strongly reduced activity compared to the wild type enzyme. The mutant improves the Cd2+ tolerance of Arabidopsis thaliana
C109A
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mutant enzyme shows similar degree of Cd2+ tolerance on DTY167 cells as the wild-type equivalent
C109S
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mutant enzyme shows similar degree of Cd2+ tolerance on DTY167 cells as the wild-type equivalent
C109Y
the mutant has strongly reduced activity compared to the wild type enzyme. The mutant improves the Cd2+ tolerance of Arabidopsis thaliana
C113A
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mutant enzyme shows similar degree of Cd2+ tolerance on DTY167 cells as the wild-type equivalent
C113S
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mutant enzyme shows similar degree of Cd2+ tolerance on DTY167 cells as the wild-type equivalent
C56S
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mutation abolishes Cd2+ tolerance observed with wild-type enzyme, causes negligible intracellular phytochelatin accumulation
C90A
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mutant enzyme shows similar degree of Cd2+ tolerance on DTY167 cells as the wild-type equivalent
C90S
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mutant enzyme shows similar degree of Cd2+ tolerance on DTY167 cells as the wild-type equivalent
C91A
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mutant enzyme shows similar degree of Cd2+ tolerance on DTY167 cells as the wild-type equivalent
C91S
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mutant enzyme shows similar degree of Cd2+ tolerance on DTY167 cells as the wild-type equivalent
C91S/A199S
the mutant has strongly reduced activity compared to the wild type enzyme. The mutant improves the Cd2+ tolerance of Arabidopsis thaliana
D180A
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the mutation abolishes Cd2+ tolerance and phytocelatin synthetic activity
D71N
the mutant has strongly reduced activity compared to the wild type enzyme. The mutant improves the Cd2+ tolerance of Arabidopsis thaliana
DELTA1-284
biosynthetically active in the presence of cadmium ions and supporting phytochelatin formation at a rate that is only about 5fold lower than that of full-length AtPCS1. The loss of the C-terminal region substantially decreases the thermal stability of the enzyme and impairs phytochelatin formation in the presence of certain heavy metals
DELTA1-373
almost as stable and biosynthetically active (in the presence of cadmium) as the full-length enzyme
DELTA222-485
truncation mutant is fulla sufficient for phytochelatin synthesis. The fragment may be insufficient to maintain the active form of the enzyme stably in vitro
E52K
the mutant has strongly reduced activity compared to the wild type enzyme. The mutant improves the Cd2+ tolerance of Arabidopsis thaliana
F83C/N170D
the mutant has strongly reduced activity compared to the wild type enzyme. The mutant improves the Cd2+ tolerance of Arabidopsis thaliana
H162A
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the mutation abolishes Cd2+ tolerance and phytocelatin synthetic activity
Q48R/C144Y/G168S/W280R
the mutant has strongly reduced activity compared to the wild type enzyme. The mutant improves the Cd2+ tolerance of Arabidopsis thaliana
R74H/S230C/L250R
the mutant has strongly reduced activity compared to the wild type enzyme. The mutant improves the Cd2+ tolerance of Arabidopsis thaliana
S51T/N143I/N170I/H220R
the mutant has strongly reduced activity compared to the wild type enzyme. The mutant improves the Cd2+ tolerance of Arabidopsis thaliana
S60C/S202I
the mutant has strongly reduced activity compared to the wild type enzyme. The mutant improves the Cd2+ tolerance of Arabidopsis thaliana
T123R/F163I
the mutant has strongly reduced activity compared to the wild type enzyme. The mutant improves the Cd2+ tolerance of Arabidopsis thaliana
T139P
the mutant has strongly reduced activity compared to the wild type enzyme. The mutant improves the Cd2+ tolerance of Arabidopsis thaliana
V181G
the mutant has strongly reduced activity compared to the wild type enzyme. The mutant improves the Cd2+ tolerance of Arabidopsis thaliana
V97C
the mutant has strongly reduced activity compared to the wild type enzyme. The mutant improves the Cd2+ tolerance of Arabidopsis thaliana
V97L
the mutant has strongly reduced activity compared to the wild type enzyme. The mutant improves the Cd2+ tolerance of Arabidopsis thaliana
Y186C
the mutant has strongly reduced activity compared to the wild type enzyme. The mutant improves the Cd2+ tolerance of Arabidopsis thaliana
R183a
AtPCS1 mutant, Arg183 is critical to the activity of PCS
R183a
AtPCS1-N mutant, Arg183 is critical to the activity of PCS
T49A
AtPCS1 mutant, Thr49 is the only residue to be phosphorylated
T49A
AtPCS1-N mutant, Thr49 is the only residue to be phosphorylated
Y55A
AtPCS1 mutant
additional information
AtPCS2-overexpressing transgenic Arabidopsis thaliana and Nicotiana tabacum plants display increased seed germination rates and seedling growth under high salt stress. Furthermore, decreased levels of hydrogen peroxide (H2O2) and lipid peroxidation are observed in transgenic Arabidopsis thaliana compared to wild-type specimens. Salt stress greatly reduces transcript levels of CuSOD2, FeSOD2, CAT2, and GR2 in wild-type but not in transgenic Arabidopsis thaliana. Levels of CAT3 in transgenic Arabidopsis are markedly increased upon salt stress, suggesting that low accumulation of H2O2 in transgenic Arabidopsis is partially achieved through induction of CAT
additional information
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AtPCS2-overexpressing transgenic Arabidopsis thaliana and Nicotiana tabacum plants display increased seed germination rates and seedling growth under high salt stress. Furthermore, decreased levels of hydrogen peroxide (H2O2) and lipid peroxidation are observed in transgenic Arabidopsis thaliana compared to wild-type specimens. Salt stress greatly reduces transcript levels of CuSOD2, FeSOD2, CAT2, and GR2 in wild-type but not in transgenic Arabidopsis thaliana. Levels of CAT3 in transgenic Arabidopsis are markedly increased upon salt stress, suggesting that low accumulation of H2O2 in transgenic Arabidopsis is partially achieved through induction of CAT
additional information
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AtPCS2-overexpressing transgenic Arabidopsis thaliana and Nicotiana tabacum plants display increased seed germination rates and seedling growth under high salt stress. Furthermore, decreased levels of hydrogen peroxide (H2O2) and lipid peroxidation are observed in transgenic Arabidopsis thaliana compared to wild-type specimens. Salt stress greatly reduces transcript levels of CuSOD2, FeSOD2, CAT2, and GR2 in wild-type but not in transgenic Arabidopsis thaliana. Levels of CAT3 in transgenic Arabidopsis are markedly increased upon salt stress, suggesting that low accumulation of H2O2 in transgenic Arabidopsis is partially achieved through induction of CAT
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additional information
Zn2+/Cd2+ concentrations in both shoots and roots of the transgenic Arabidopsis seedlings expressing PCS1 and/or PCS2 are higher than in wild-type seedlings at two different Zn2+/Cd2+ concentrations. In addition, there is a positive correlation between Zn2+ accumulation and the expression level of MnPCS1 or MnPCS2
additional information
Zn2+/Cd2+ concentrations in both shoots and roots of the transgenic Arabidopsis seedlings expressing PCS1 and/or PCS2 are higher than in wild-type seedlings at two different Zn2+/Cd2+ concentrations. In addition, there is a positive correlation between Zn2+ accumulation and the expression level of MnPCS1 or MnPCS2
additional information
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Zn2+/Cd2+ concentrations in both shoots and roots of the transgenic Arabidopsis seedlings expressing PCS1 and/or PCS2 are higher than in wild-type seedlings at two different Zn2+/Cd2+ concentrations. In addition, there is a positive correlation between Zn2+ accumulation and the expression level of MnPCS1 or MnPCS2
additional information
an extra copy of phytochelatin-encoding gene phytochelatin synthase (pcs) is constitutively expressed in Anabaena sp. strain PCC7120 (An7120), an integrative expression vector pFPN is used for incorporating a cassette of genes for genomic integration and expression. Comparative growth behavior of wild-type strain and overexpressed strain AnFPN-pcs under LC50 doses of UV-B, salt, heat, copper, carbofuran, and cadmium resulted in decrement in specific growth rate by 26, 21, 27, 13, 30, and 17%, respectively, in An7120 compared to AnFPN-pcs thereby suggesting that the transformed cyanobacterium AnFPN-pcs has developed tolerance and hence shows better growth performances under different abiotic stresses. Comparison of differentially expressed proteins in An7120 and AnFPN-pcs, and dynamics of differentially expressed proteins in An7120 and AnFPN-pcs, overview
additional information
analysis of the transgenic rice lines grown under metal(loid) stress revealed almost complete absence of both OsPCS1 and OsPCS2 transcripts in the developing seeds couples with the significant reduction in the content of Cd (about 51%) and As (about 35%) in grains compared with the non-transgenic plant. Taken together, the findings indicate towards a crucial role played by the tissue-specific alternative splicing and relative abundance of the OsPCS2 gene during heavy metal(loid) stress mitigation in rice plant
additional information
analysis of the transgenic rice lines grown under metal(loid) stress revealed almost complete absence of both OsPCS1 and OsPCS2 transcripts in the developing seeds couples with the significant reduction in the content of Cd (about 51%) and As (about 35%) in grains compared with the non-transgenic plant. Taken together, the findings indicate towards a crucial role played by the tissue-specific alternative splicing and relative abundance of the OsPCS2 gene during heavy metal(loid) stress mitigation in rice plant
additional information
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analysis of the transgenic rice lines grown under metal(loid) stress revealed almost complete absence of both OsPCS1 and OsPCS2 transcripts in the developing seeds couples with the significant reduction in the content of Cd (about 51%) and As (about 35%) in grains compared with the non-transgenic plant. Taken together, the findings indicate towards a crucial role played by the tissue-specific alternative splicing and relative abundance of the OsPCS2 gene during heavy metal(loid) stress mitigation in rice plant
additional information
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analysis of the transgenic rice lines grown under metal(loid) stress revealed almost complete absence of both OsPCS1 and OsPCS2 transcripts in the developing seeds couples with the significant reduction in the content of Cd (about 51%) and As (about 35%) in grains compared with the non-transgenic plant. Taken together, the findings indicate towards a crucial role played by the tissue-specific alternative splicing and relative abundance of the OsPCS2 gene during heavy metal(loid) stress mitigation in rice plant
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additional information
identification of two independent OsPCS1 mutant rice lines, a T-DNA and a Tos17 insertion line. The mutant rice plants grown in soil with environmentally relevant As and Cd concentrations show increased As accumulation and decreased Cd accumulation in grains of the T-DNA line. The Tos17 mutant also exhibits the reduced Cd accumulation phenotype. These contrasting effects on As and Cd distribution to grains suggest the existence of at least partially distinct PC-dependent pathways for As and Cd
additional information
identification of two independent OsPCS1 mutant rice lines, a T-DNA and a Tos17 insertion line. The mutant rice plants grown in soil with environmentally relevant As and Cd concentrations show increased As accumulation and decreased Cd accumulation in grains of the T-DNA line. The Tos17 mutant also exhibits the reduced Cd accumulation phenotype. These contrasting effects on As and Cd distribution to grains suggest the existence of at least partially distinct PC-dependent pathways for As and Cd
additional information
identification of two independent OsPCS1 mutant rice lines, a T-DNA and a Tos17 insertion line. The mutant rice plants grown in soil with environmentally relevant As and Cd concentrations show increased As accumulation and decreased Cd accumulation in grains of the T-DNA line. The Tos17 mutant also exhibits the reduced Cd accumulation phenotype. These contrasting effects on As and Cd distribution to grains suggest the existence of at least partially distinct PC-dependent pathways for As and Cd
additional information
identification of two independent OsPCS1 mutant rice lines, a T-DNA and a Tos17 insertion line. The mutant rice plants grown in soil with environmentally relevant As and Cd concentrations show increased As accumulation and decreased Cd accumulation in grains of the T-DNA line. The Tos17 mutant also exhibits the reduced Cd accumulation phenotype. These contrasting effects on As and Cd distribution to grains suggest the existence of at least partially distinct PC-dependent pathways for As and Cd
additional information
identification of two independent OsPCS1 mutant rice lines, a T-DNA and a Tos17 insertion line. The mutant rice plants grown in soil with environmentally relevant As and Cd concentrations show increased As accumulation and decreased Cd accumulation in grains of the T-DNA line. The Tos17 mutant also exhibits the reduced Cd accumulation phenotype. These contrasting effects on As and Cd distribution to grains suggest the existence of at least partially distinct PC-dependent pathways for As and Cd
additional information
identification of two independent OsPCS1 mutant rice lines, a T-DNA and a Tos17 insertion line. Thee mutant rice plants grown in soil with environmentally relevant As and Cd concentrations show increased As accumulation and decreased Cd accumulation in grains of the T-DNA line. The Tos17 mutant also exhibits the reduced Cd accumulation phenotype. These contrasting effects on As and Cd distribution to grains suggest the existence of at least partially distinct PC-dependent pathways for As and Cd
additional information
identification of two independent OsPCS1 mutant rice lines, a T-DNA and a Tos17 insertion line. Thee mutant rice plants grown in soil with environmentally relevant As and Cd concentrations show increased As accumulation and decreased Cd accumulation in grains of the T-DNA line. The Tos17 mutant also exhibits the reduced Cd accumulation phenotype. These contrasting effects on As and Cd distribution to grains suggest the existence of at least partially distinct PC-dependent pathways for As and Cd
additional information
identification of two independent OsPCS1 mutant rice lines, a T-DNA and a Tos17 insertion line. Thee mutant rice plants grown in soil with environmentally relevant As and Cd concentrations show increased As accumulation and decreased Cd accumulation in grains of the T-DNA line. The Tos17 mutant also exhibits the reduced Cd accumulation phenotype. These contrasting effects on As and Cd distribution to grains suggest the existence of at least partially distinct PC-dependent pathways for As and Cd
additional information
identification of two independent OsPCS1 mutant rice lines, a T-DNA and a Tos17 insertion line. Thee mutant rice plants grown in soil with environmentally relevant As and Cd concentrations show increased As accumulation and decreased Cd accumulation in grains of the T-DNA line. The Tos17 mutant also exhibits the reduced Cd accumulation phenotype. These contrasting effects on As and Cd distribution to grains suggest the existence of at least partially distinct PC-dependent pathways for As and Cd
additional information
identification of two independent OsPCS1 mutant rice lines, a T-DNA and a Tos17 insertion line. Thee mutant rice plants grown in soil with environmentally relevant As and Cd concentrations show increased As accumulation and decreased Cd accumulation in grains of the T-DNA line. The Tos17 mutant also exhibits the reduced Cd accumulation phenotype. These contrasting effects on As and Cd distribution to grains suggest the existence of at least partially distinct PC-dependent pathways for As and Cd
additional information
isolation of two rice mutants (has1 and has2) in which As levels are much higher in grains but significantly lower in node I compared with the wild-type. Map-based cloning identifies the genes responsible as OsABCC1 in has1 and OsPCS1 in has2. F2 progeny obtained by crossing the mutant lines with the indica rice cultivar Habataki are genotyped by using polymorphism between cvs. Koshihikari and Habataki and measurements of As levels in grains from the F2 plants. The frequency of the high-As phenotype in F2 progeny is below 50%, suggesting that has1 and has2 are recessive mutants. Genetic linkage analyses indicate that the high-As mutant phenotypes are tightly linked to single regions on chromosome 4 in has1 and on chromosome 5 in has2
additional information
isolation of two rice mutants (has1 and has2) in which As levels are much higher in grains but significantly lower in node I compared with the wild-type. Map-based cloning identifies the genes responsible as OsABCC1 in has1 and OsPCS1 in has2. F2 progeny obtained by crossing the mutant lines with the indica rice cultivar Habataki are genotyped by using polymorphism between cvs. Koshihikari and Habataki and measurements of As levels in grains from the F2 plants. The frequency of the high-As phenotype in F2 progeny is below 50%, suggesting that has1 and has2 are recessive mutants. Genetic linkage analyses indicate that the high-As mutant phenotypes are tightly linked to single regions on chromosome 4 in has1 and on chromosome 5 in has2
additional information
silencing of OsPCS1 expression via RNA interference by OsPCS1 RNAi introduced into rice via Agrobacterium tumefaciens strain EHA105 transfection method. Phenotypes, overview
additional information
silencing of OsPCS1 expression via RNA interference by OsPCS1 RNAi introduced into rice via Agrobacterium tumefaciens strain EHA105 transfection method. Phenotypes, overview
additional information
silencing of OsPCS2 expression via RNA interference by OsPCS2 RNAi introduced into rice via Agrobacterium tumefaciens strain EHA105 transfection method. Phenotypes, overview
additional information
silencing of OsPCS2 expression via RNA interference by OsPCS2 RNAi introduced into rice via Agrobacterium tumefaciens strain EHA105 transfection method. Phenotypes, overview
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AtPCS2-gene expressed in Saccharomyces cerevisiae strain INVSc1
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AtPCS2-gene expressed in Schizosaccharomyces pombe strain FY254, a phytochelatin synthase knockout strain
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BjPCS1 is expressed in Escherichia coli
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expressed in a Arabidopsis thaliana cad1-3 phytochelatin-deficient mutant and in Nicotiana tabacum cultivar Petit Havana
expressed in Arabidopsis thaliana via transformation with Agrobacterium tumefaciens strain EHA105
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expressed in Brassica juncea
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expressed in Escherichia coli
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expressed in Escherichia coli BL21 Rosetta (DE3) pLysS cells
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expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3) cells and Saccharomyces cerevisiae strain TY167
expressed in Escherichia coli Rosetta (DE3) cells
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expressed in Nicotiana tabacum
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expressed in Nicotiana tabacum and Saccharomyces cerevisiae
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expressed in Saccharomyces cerevisiae
expressed in Saccharomyces cerevisiae strain BY4741
expressed in Saccharomyces cerevisiae strain BY4742
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expressed in Saccharomyces cerevisiae strain YK44 and Nicotiana tabacum strain NC89
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expressed in Schizosaccharomyces pombe strain SP27, a phytochelatin synthase knockout strain
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expression in Escherichia coli and Saccharomyces cerevisiae to enhance tolerance to toxicity of cadmium ion
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expression in Mesorhizobium huakuii subsp. rengei B3. The PCS(At) gene is expressed under the control of the nifH promoter, which regulates the nodule-specific expression of nifH gene. Expression of the PCS(At) gene in Mesorhizobium huakuii subsp. rengei B3 increases the ability of cells to bind Cd2+ approximately 9fold to 19fold
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expression in Saccharomyces cerevisiae
expression in Saccharomyces cerevisiae. Yeast cells expressing LjPCS3 show increased in vivo tolerance to Cd
fused to a C-terminal Flag epitope
gene alr0975 or pcs, DNA and amino acid sequence determination and analysis, recombinant expression in Escherichia coli strain DH5alpha, and functional constitutive overexpression in Anabaena sp. strain PCC 7120, semiquantitative RT-PCR enzyme expression analysis
gene CaPCS1, DNA and amino acid sequence determination and analysis, sequence comparisons, phylogenetic analysis, genotyping, recombinant expression in Escherichia coli improves the cadmium resistance of the bacteria, quantitative RT-PCR enzyme expression analysis
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gene CaPCS2, DNA and amino acid sequence determination and analysis, sequence comparisons, phylogenetic analysis, genotyping, recombinant expression in Escherichia coli improves the cadmium resistance of the bacteria, quantitative RT-PCR enzyme expression analysis
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gene DaPCS1, DNA and amino acid sequence determination and analysis, sequence comparisons, phylogenetic analysis, genotyping, recombinant expression in Escherichia coli, quantitative RT-PCR enzyme expression analysis
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gene OsPCS1, recombinant expression in Escherichia coli, recombinant expression of MBP-tagged OsPCS1 in the has2 mutant under the control of the cauliflower mosaic virus (CaMV) 35S promoter, the nodes of the OsPCS1-overexpressing line show higher As levels than those of the wild-type
gene OsPCS2, recombinant expression in Escherichia coli, recombinant expression of MBP-tagged OsPCS1 in the has2 mutant under the control of the cauliflower mosaic virus (CaMV) 35S promoter. Overexpression of OsPCS2 does not fully complement the has2 mutation, although the As levels in grains became lower than in the non-transgenic has2 mutant
gene PCS1, DNA and amino acid sequence determination and analysis, sequence comparisons, different PCS1 splicing variants are detected, quantitative expression analysis, recombinant expression of MBP-tagged isozyme PCS1
gene PCS1, isolation of four different transcript variants of OsPCS1, and amino acid sequence determination and analysis, quantitative real-time RT-PCR enzyme expression analysis revealing that expression of the longest OsPCS1 variant, OsPCS1full, is most abundant, functional recombinant in expression in PCS-deficient
gene PCS1, isolation of four different transcript variants of OsPCS1, and amino acid sequence determination and analysis, quantitative real-time RT-PCR enzyme expression analysis revealing that expression of the longest OsPCS1 variant, OsPCS1full, is most abundant, functional recombinant in expression in PCS-deficient mutants of Schizosaccharomyces pombe PCS knockout strain DELTApcs and Arabidopsis thaliana null mutant cad1-3 plants with OsPCS1full possessing good PCS activity in response to As(III) and Cd while the activity of the other PCS variants is very low
gene PCS1, isolation of four different transcript variants of OsPCS1, and amino acid sequence determination and analysis, quantitative real-time RT-PCR enzyme expression analysis revealing that expression of the longest OsPCS1 variant, OsPCS1full, is most abundant, functional recombinant in expression in PCS-deficient mutants of Schizosaccharomyces pombe PCS knockout strain DELTApcs and Arabidopsis thaliana null mutant cad1-3 plants with OsPCS1full possessing good PCS activity in response to As(III) and Cd while the activity of the other PCS variants is very low. Transcript of the introduced OsPCS genes is evident in all cad1-3/OsPCS lines except for cad1-3/OsPCS1b line
gene PCS1, isolation of four different transcript variants of OsPCS1, DNA and amino acid sequence determination and analysis, quantitative real-time RT-PCR enzyme expression analysis revealing that expression of the longest OsPCS1 variant, OsPCS1full, is most abundant, functional recombinant in expression in PCS-deficient mutants of Schizosaccharomyces pombe PCS knockout strain DELTApcs and Arabidopsis thaliana null mutant cad1-3 plants with OsPCS1full possessing good PCS activity in response to As(III) and Cd while the activity of the other PCS variants is very low. Phenotypes, overview
gene PCS1, recombinant expression in Escherichia coli strain Rosetta (DE3) pLysS
gene PCS1, sequence comparisons and phylogenetic analysis, recombinant expression in Arabidopsis thaliana Col-0 ecotype, and induction by Cd2+, functional recombinant expression in Saccharomyces cerevisiae YK44 highly Cd2+-sensitive strain conferring Cd resistance. Compared to PCS2 and 3 expressing lines, the AdPCS1 transformant has a longer lag phase, resulting in slower initial growth. This difference is rescued after 24 h, with the growth kinetics of the AdPCS1 transformant becoming normal, indicating that the difference results from decreased translational efficiency
gene PCS1, two Morus notabilis PCS genes are identified based on a genome-wide analysis of the Morus genome database, DNA and amino acid sequence determination and analysis, exon-intron structures of the MnPCS genes, quantitative real-time PCR enzyme expression analysis, expression in Arabidopsis thaliana
gene PCS15, DNA and amino acid sequence determinataion and analysis, RT-PCR expression analysis, recombinant expression in Saccharomyces cerevisiae ycf1 mutant (DELTAycf1) cells (DTY167) confers Cd resistance. The growth of OsPCS15-transformed DELTAycf1 cells is similar to that of empty vector-transformed wild-type and DELTAycf1 cells. Recombinant overexpression of GFP-tagged enzyme PCS15 in Arabidopsis thaliana under control of the CaMV 35S promoter leading to increasing Cd2+ concentrations. Root growth in OsPCS15 transgenic plants is reduced by approximately 26% following treatment with 0.05-0.07 mM CdCl2. In contrast, ectopic expression of PCS15 increases the sensitivity to Cd in Arabidopsis thaliana
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gene PCS2, DNA and amino acid sequence determination and analysis, chromosome 6, genomic organization of OsPCS1 constitutes 5 exons separated by 4 introns, whereas that of OsPCS2 indicates the presence of 6 exons interrupted by 5 introns. Quantitative RT-PCR expression analysis. Among the two PCS genes, OsPCS1 and OsPCS2 in indica rice cultivar, the OsPCS2 produces an alternatively spliced OsPCS2b transcript that bears the unusual premature termination codon besides the canonically spliced OsPCS2a transcript. Root- and shoot-specific differential ratios of alternatively spliced OsPCS2a and OsPCS2b transcript expressions are observed under cadmium stress, recombinant expression in Saccharomyces cerevisiae cells transformed with OsPCS2a exhibits increased cadmium and arsenic tolerance and accumulation, unlike the OsPCS2b transformed yeast cells
gene PCS2, DNA and amino acid sequence determination and analysis, sequence comparisons, different PCS1 splicing variants are detected, quantitative expression analysis, recombinant expression of MBP-tagged isozyme PCS2
gene PCS2, isolation of a single transcript form of OsPCS2, and amino acid sequence determination and analysis, quantitative real-time RT-PCR enzyme expression analysis, functional recombinant in expression in PCS-deficient mutants of Schizosaccharomyces pombe PCS knockout strain DELTApcs and Arabidopsis thaliana null mutant cad1-3 plants, the activity of PCS2 in response to As(III) and Cd is very low
gene PCS2, recombinant expression in Arabidopsis thaliana and Nicotiana tabacum var. Xanthi plants using the Agrobacterium tumefaciens strain GV3101 transfection method
gene PCS2, sequence comparisons and phylogenetic analysis, recombinant expression in Arabidopsis thaliana Col-0 ecotype, and induction by Cd2+, functional recombinant expression in Saccharomyces cerevisiae YK44 highly Cd-sensitive strain conferring Cd2+ resistance
gene PCS2, two Morus notabilis PCS genes are identified based on a genome-wide analysis of the Morus genome database, DNA and amino acid sequence determination and analysis, exon-intron structures of the MnPCS genes, quantitative real-time PCR enzyme expression analysis, recombinant expression in Arabidopsis thaliana
gene PCS3, sequence comparisons and phylogenetic analysis, recombinant expression in Arabidopsis thaliana Col-0 ecotype, and induction by Cd2+, functional recombinant expression in Saccharomyces cerevisiae YK44 highly Cd-sensitive strain conferring Cd2+ resistance
gene PCS5, DNA and amino acid sequence determinataion and analysis, RT-PCR expression analysis, recombinant expression in Saccharomyces cerevisiae ycf1 mutant (DELTAycf1) cells (DTY167) confers Cd resistance. The growth of OsPCS5-transformed DELTAycf1 cells is similar to that of empty vector-transformed wild-type and DELTAycf1 cells. Recombinant overexpression of GFP-tagged enzyme PCS5 in Arabidopsis thaliana under control of the CaMV 35S promoter leading to increasing Cd2+ concentrations. Root growth in OsPCS5 transgenic plants is reduced by approximately 33% following treatment with 0.05-0.07 mM CdCl2. In contrast, ectopic expression of PCS5 increases the sensitivity to Cd in Arabidopsis thaliana
-
heterologous expression of AtPCS1-FLAG in Saccharomyces cerevisiae
-
heterologously expressed in Escherichia coli
into the binary plasmid vector pCB302 for introducing into Agrobacterium GV3101 strain, tobacco plants are transformed by the standard leaf disc method
into the pGEM-T easy vector for sequencing, into the vector pYES2 for expression in Saccharomyces cerevisiae cells
into the vector pET-28b for expression in Escherichia coli BL21 Rosetta DE3 pLysS cells
overexpressed in transgenic Arabidopsis thaliana
-
overexpression both in wild-type and rolB-transformed Nicotiana tabacum. Increase in Cd2+ tolerance and accumulation in the overexpressing plants is directly related to the availability of reduced glutathione, while overexpression of phytochelatin synthase does not enhance long distance root-to shoot Cd2+ transport
-
overexpression in Arabidopsis from a strong constitutive Arabidopsis actin regulatory sequence (A2), the A2::AtPCS1 plants are highly resistant to arsenic, accumulating 20-100times more biomass on 0.25 and 0.3 mM arsenate than wild-type, however, they are hypersensitive to Cd(II). After exposure to cadmium and arsenic, the overall accumulation of thiol-peptides increases to 10fold higher levels in the A2::AtPCS1 plants compared with wild-type
-
overexpression of AtPCS1 in transgenic Arabidopsis. Transgenic plants with a relatively high level of expression of the 35S::AtPCS1 transgene does not result in higher Cd tolerance, but rather show higher sensitivity to Cd under some conditions. Transgenic plants showing a relatively lower level of expression of the 35S::AtPCS1 transgene show increased accumulation and tolerance of Cd compared to wild-type plants
-
the coding sequences of full-length PCS1, PCS-N, residues 1-221, and PCS-C, residues 222-485, are cloned into the vector pGEM-T-Easy and subsequently into pET28b for expression in Escherichia coli BL21DE3 cells
the plasmid pYES3-AtPCS1-FLAG is used for the transformation of Saccharomyces cerevisiae cells
-
transformed into Saccharomyces cerevisiae DTY167
transformed into Saccharomyces cerevisiae strain DTY67, hypersensitive to Cd2+-stress
G5ECE4
with the TOPO TA Cloning kit for sequencing
-
-
expressed in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3) cells
expressed in Saccharomyces cerevisiae
-
expressed in Saccharomyces cerevisiae
-
expressed in Saccharomyces cerevisiae
expressed in Saccharomyces cerevisiae strain BY4741
expressed in Saccharomyces cerevisiae strain BY4741
fused to a C-terminal Flag epitope
-
fused to a C-terminal Flag epitope
heterologously expressed in Escherichia coli
-
heterologously expressed in Escherichia coli
into the binary plasmid vector pCB302 for introducing into Agrobacterium GV3101 strain, tobacco plants are transformed by the standard leaf disc method
-
into the binary plasmid vector pCB302 for introducing into Agrobacterium GV3101 strain, tobacco plants are transformed by the standard leaf disc method
-
transformed into Saccharomyces cerevisiae DTY167
-
transformed into Saccharomyces cerevisiae DTY167
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88-96
2018
Nitella mucronata
brenda
Chaurasia, N.; Mishra, Y.; Chatterjee, A.; Rai, R.; Yadav, S.; Rai, L.C.
Overexpression of phytochelatin synthase (pcs) enhances abiotic stress tolerance by altering the proteome of transformed Anabaena sp. PCC 7120
Protoplasma
254
1715-1724
2017
Nostoc sp. PCC 7120 = FACHB-418 (Q8YY76)
brenda
Zhang, D.; Yamamoto, T.; Tang, D.; Kato, Y.; Horiuchi, S.; Ogawa, S.; Yoshimura, E.; Suzuki, M.
Enhanced biosynthesis of CdS nanoparticles through Arabidopsis thaliana phytochelatin synthase-modified Escherichia coli with fluorescence effect in detection of pyrogallol and gallic acid
Talanta
195
447-455
2019
Arabidopsis thaliana (Q9S7Z3), Arabidopsis thaliana
brenda