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On June 7, 2022, the research paper
entitled "Structural basis for MTA1c-mediated DNA N6-adenine methylation" was published online in Nature Communications.
DNA methylation plays a pivotal role
in biological growth and development as well as in human health and disease development.
The study found that compared with multicellular eukaryotes, the tetrahymene genome 6mA modification content is high, and mainly concentrated in the transcriptional initiation region
.
In order to reveal the function and regulatory mechanism of eukaryotic DNA 6mA methylation, this study started from the thermophilic tetrahymens MTA1c complex, combined with biochemistry, molecular biology and structural biology research methods and techniques, by analyzing the structure of multiple MTA1c-related complexes, it was found that MTA1 is the core protein and catalytic subunit of the MTA1c complex, which can interact with MTA9, p1 and p2 respectively, thereby driving the assembly
of the MTA1c quaternary complex 。 MTA1 is in a self-inhibiting conformation when not bound to p2 and does not bind to the methyl donor-SAT; After binding to p2, the self-suppressing conformation of MTA1 is lifted
.
MTA1c identifies the structural basis of SAM and SAH
In addition, this study found that MTA1, MTA9, p1 and p2 can form a special DNA-binding channel by structural assembly, and all four proteins are involved in the specific recognition of substrate DNA, but in the end only MTA1 is used to catalyze the transfer
of methyl from SAM to DNA adenine N6.
MTA1c identifies a structural model of substrate DNA
In this work, the atomic structure of the Thermophilic Tetrahymens DNA 6mA methyltransferase complex was resolved for the first time, and the molecular mechanism
of MTA1c-catalyzed DNA 6mA methylation in eukaryotes was systematically studied.
Chen Jiyun, assistant professor of Liu Liang's research group, Hu Rong, a 2017 doctoral candidate, Chen Ying, a 2020 master's student, and Lin Xiaofeng, a 2020 master's student, are the co-first authors
of this paper.
Original link:
