Dependence of wheat endonuclease -WEN1 on S-Adenosyl-L-Methionine (S-AdoMet) and its sensitivity to DNA methylation status
Student name: Tseng Chu-Yun (Ally)
ID:42094719
Abstract:
Wheat WEN1 endonuclease purified from aging coleoptiles with molecular weight of around 27 kDa was Ca++- and Mg++-dependent. Cleavage of methylated lambda phage (dam+, dcm+) DNA by WEN1 was more efficient than that of unmethylated lambda phage (dam-, dcm-) DNA by WEN1. Whilst double-stranded DNA (dsDNA) was cleaved, two activity peaks of pH values (pH 6.5-7.5 and pH9.0-10.5) emerged. WEN1 appeared to be stable in a wide scope of pH and at elevated temperature such as 65°C. Activation of WEN1 endonuclease could be achieved by S-adenosyl-L-methionine, S-adenosyl-L-homocysteine and S-isobutyladenosine. Significantly, it is the first case to verify that endonuclease of higher eukaryote is able to differentiate between different methylation statuses of DNA and is modulated by S-adenosyl-L-methionine (S-AdoMet) and its analogs.
ID:42094719
Abstract:
Wheat WEN1 endonuclease purified from aging coleoptiles with molecular weight of around 27 kDa was Ca++- and Mg++-dependent. Cleavage of methylated lambda phage (dam+, dcm+) DNA by WEN1 was more efficient than that of unmethylated lambda phage (dam-, dcm-) DNA by WEN1. Whilst double-stranded DNA (dsDNA) was cleaved, two activity peaks of pH values (pH 6.5-7.5 and pH9.0-10.5) emerged. WEN1 appeared to be stable in a wide scope of pH and at elevated temperature such as 65°C. Activation of WEN1 endonuclease could be achieved by S-adenosyl-L-methionine, S-adenosyl-L-homocysteine and S-isobutyladenosine. Significantly, it is the first case to verify that endonuclease of higher eukaryote is able to differentiate between different methylation statuses of DNA and is modulated by S-adenosyl-L-methionine (S-AdoMet) and its analogs.
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