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2020, Vol.49, No.7

785-788

The Dynamics of S-adenosyl-methionine and S-adenosyl-homocysteine in Mouse Dnmt1 is Driven by Their Structural Flexibilities

Takunori Yasuda ,1Yasuteru Shigeta ,2 and Ryuhei Harada *2
1College of Biological Sciences, University of Tsukuba, 1-1-1 Tennodai, Tsukuba, Ibaraki 305-0821, Japan
2Center for Computational Sciences, University of Tsukuba, 1-1-1 Tennodai, Tsukuba, Ibaraki 305-0821, Japan
https://doi.org/10.1246/cl.200223

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Abstract

DNA methyl transferase1 (Dnmt1) preferentially methylates hemi-methylated DNA. Upon the methylation of DNA, a methyl group is provided by S-adenosyl-l-methionine (SAM), which becomes the product S-adenosyl-l-homocysteine (SAH). We performed molecular dynamics (MD) simulations to trace the dynamics of SAM and address SAH in inactivated Dnmt1 in mice. Our MD simulations found that SAM was more stable than SAH under the inactivated Dnmt1 environment, indicating that an exchange of cofactors might occur in the inactivation state before the next methylation process.

figure

DNA methyl transferase1 (Dnmt1) is an enzyme which preferentially methylates hemi-methylated DNA. A methyl group is provided by S-adenosyl-l-methionine (SAM), which becomes S-adenosyl-l-homocysteine (SAH). Our MD simulations showed that SAM was more stable than SAH in the inactivated Dnmt1, indicating that an exchange of the cofactors might have occurred in the inactivation state before the next methylation process.

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