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Research Paper
Wheat Endonuclease WEN1 Dependent on S-Adenosyl-L-Methionine and Sensitive to DNA Methylation Status
Larisa I. Fedoreyeva, Dmitriy E. Sobolev and Boris F. Vanyushin
volume 2 | issue 1
january/february/march 2007Pages: 50 - 53
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Ca2+-, Mg2+-dependent wheat endonuclease WEN1 with molecular mass of about 27 kDa was isolated from coleoptyles. Methylated DNA of λ phage grown on E. coli dam+, dcm+ cells was hydrolyzed by WEN1 more effectively than DNA of phage grown on dam , dcm- cells. Two pH activity maxima (pH 6.5-7.5 and 9.0-10.5) were observed when double-stranded DNA was hydrolyzed. WEN1 is stable at elevated temperatures (65оС) and in wide range of pH values. WEN1 is activated by S-adenosyl-L-methionine, S-adenosyl-L-homocysteine and S-izobutyladenosine. It is a first case to show that higher eukaryote endonuclease discriminates between DNA of various methylation status and is modulated by S-AdoMet and its analogs.
Authors
Larisa I. Fedoreyeva
Lomonosov Moscow State University, Moscow, Russia
Dmitriy E. Sobolev
Lomonosov Moscow State University, Moscow, Russia
Boris F. Vanyushin
Lomonosov Moscow State University, Moscow, Russia
We now provide open access to journal articles published online for one year or more. This article may be downloaded at the following link:
Download PDF If the document does not open, please right-click on the link (control-click on a Macintosh) and select the option to save the file to disk.