OsPCS2

• Symbol: OsPCS2
• MSU: LOC_Os06g01260
• RAPdb: Os06g0102300

• Identification of alternatively spliced transcripts of rice phytochelatin synthase 2 gene OsPCS2 involved in mitigation of cadmium and arsenic stresses., 2017, Plant Mol Biol.
• Domain exchange between Oryza sativa phytochelatin synthases reveals a region that determines responsiveness to arsenic and heavy metals., 2020, Biochem Biophys Res Commun.

Genbank accession number

• The OsPCS2 exhibits root- and shoot-specific differential ratios of alternatively spliced transcripts in indica rice under Cd stress, and plays role in Cd and As stress tolerance and accumulation
• 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 coupled with the significant reduction in the content of Cd (~51%) and As (~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
• Identification of alternatively spliced transcripts of rice phytochelatin synthase 2 gene OsPCS2 involved in mitigation of cadmium and arsenic stresses.
• ) has two PCSs (OsPCS1 and OsPCS2), and we previously revealed that OsPCS1 has a higher responsiveness to arsenic than to cadmium, while OsPCS2 has a higher responsiveness to cadmium than to arsenic
• A chimeric protein in which the 183<U+00A0>C-terminal amino acids of OsPCS2 were replaced with the 185<U+00A0>C-terminal amino acids of OsPCS1 showed higher responsiveness to arsenite than to cadmium, similar to OsPCS1

• OsPCS1, OsPCS2, Phytochelatin synthase OsPCS1 plays a crucial role in reducing arsenic levels in rice grains., The levels of As in grains and node I were similar between the two mutants, suggesting that OsABCC1 preferentially cooperates with OsPCS1 to sequester As, although rice has another phytochelatin synthase, OsPCS2
• OsPCS1, OsPCS2, Phytochelatin synthase OsPCS1 plays a crucial role in reducing arsenic levels in rice grains., In vitro phytochelatin synthesis assay indicated that OsPCS1 was more sensitive to activation by As than by cadmium, whereas OsPCS2 was more weakly activated by As than by cadmium
• OsPCS1, OsPCS2, Phytochelatin synthase has contrasting effects on cadmium and arsenic accumulation in rice grains., First, we isolated four different transcript variants of OsPCS1 as well as one from OsPCS2
• OsPCS1, OsPCS2, Phytochelatin synthase has contrasting effects on cadmium and arsenic accumulation in rice grains., Quantitative RT-PCR of each OsPCS transcript in rice seedlings suggested that expression of OsPCS1full, the longest OsPCS1 variant, was most abundant, followed by OsPCS2
• OsPCS1, OsPCS2, Domain exchange between Oryza sativa phytochelatin synthases reveals a region that determines responsiveness to arsenic and heavy metals., ) has two PCSs (OsPCS1 and OsPCS2), and we previously revealed that OsPCS1 has a higher responsiveness to arsenic than to cadmium, while OsPCS2 has a higher responsiveness to cadmium than to arsenic
• OsPCS1, OsPCS2, Domain exchange between Oryza sativa phytochelatin synthases reveals a region that determines responsiveness to arsenic and heavy metals., We constructed chimeric proteins between OsPCS1 and OsPCS2 and performed an in<U+00A0>vitro phytochelatin synthesis assay
• OsPCS1, OsPCS2, Domain exchange between Oryza sativa phytochelatin synthases reveals a region that determines responsiveness to arsenic and heavy metals., A chimeric protein in which the 183<U+00A0>C-terminal amino acids of OsPCS2 were replaced with the 185<U+00A0>C-terminal amino acids of OsPCS1 showed higher responsiveness to arsenite than to cadmium, similar to OsPCS1
• OsPCS1, OsPCS2, Domain exchange between Oryza sativa phytochelatin synthases reveals a region that determines responsiveness to arsenic and heavy metals., Contrary to expectations, mutations of cysteine residues that are unique to OsPCS1 or OsPCS2 had little influence on the responsiveness, although cysteine residues are reported to be representative of sites that interact with metals/metalloids