Structural insight into human N6amt1-Trm112 complex functioning as a protein methyltransferase.

ABSTRACT: DNA methylation is an important epigenetic modification in many organisms and can occur on cytosine or adenine. N⁶-methyladenine (6mA) exists widespreadly in bacterial genomes, which plays a vital role in the bacterial restriction-modification system. Recently, 6mA has also been reported to exist in the genomes of a variety of eukaryotes from unicellular organisms to metazoans. There were controversial reports on whether human N6amt1, which was originally reported as a glutamine MTase for eRF1, is a putative 6mA DNA MTase. We report here the crystal structure of human N6amt1-Trm112 in complex with cofactor SAM. Structural analysis shows that Trm112 binds to a hydrophobic surface of N6amt1 to stabilize its structure but does not directly contribute to substrate binding and cataly

SUBMITTER: Li W 

PROVIDER: S-EPMC6796863 | biostudies-literature | 2019

REPOSITORIES: biostudies-literature