| Title |
Solution structure of the RNA recognition domain of METTL3-METTL14 N6-methyladenosine methyltransferase
|
|---|---|
| Published in |
Protein & Cell, March 2018
|
| DOI | 10.1007/s13238-018-0518-7 |
| Pubmed ID | |
| Authors |
Jinbo Huang, Xu Dong, Zhou Gong, Ling-Yun Qin, Shuai Yang, Yue-Ling Zhu, Xiang Wang, Delin Zhang, Tingting Zou, Ping Yin, Chun Tang |
| Abstract |
N6-methyladenosine (m6A), a ubiquitous RNA modification, is installed by METTL3-METTL14 complex. The structure of the heterodimeric complex between the methyltransferase domains (MTDs) of METTL3 and METTL14 has been previously determined. However, the MTDs alone possess no enzymatic activity. Here we present the solution structure for the zinc finger domain (ZFD) of METTL3, the inclusion of which fulfills the methyltransferase activity of METTL3-METTL14. We show that the ZFD specifically binds to an RNA containing 5'-GGACU-3' consensus sequence, but does not to one without. The ZFD thus serves as the target recognition domain, a structural feature previously shown for DNA methyltransferases, and cooperates with the MTDs of METTL3-METTL14 for catalysis. However, the interaction between the ZFD and the specific RNA is extremely weak, with the binding affinity at several hundred micromolar under physiological conditions. The ZFD contains two CCCH-type zinc fingers connected by an anti-parallel β-sheet. Mutational analysis and NMR titrations have mapped the functional interface to a contiguous surface. As a division of labor, the RNA-binding interface comprises basic residues from zinc finger 1 and hydrophobic residues from β-sheet and zinc finger 2. Further we show that the linker between the ZFD and MTD of METTL3 is flexible but partially folded, which may permit the cooperation between the two domains during catalysis. Together, the structural characterization of METTL3 ZFD paves the way to elucidate the atomic details of the entire process of RNA m6A modification. |
X Demographics
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Geographical breakdown
| Country | Count | As % |
|---|---|---|
| Mexico | 1 | 50% |
| United States | 1 | 50% |
Demographic breakdown
| Type | Count | As % |
|---|---|---|
| Members of the public | 1 | 50% |
| Science communicators (journalists, bloggers, editors) | 1 | 50% |
Mendeley readers
The data shown below were compiled from readership statistics for 88 Mendeley readers of this research output. Click here to see the associated Mendeley record.
Geographical breakdown
| Country | Count | As % |
|---|---|---|
| Unknown | 88 | 100% |
Demographic breakdown
| Readers by professional status | Count | As % |
|---|---|---|
| Student > Ph. D. Student | 16 | 18% |
| Student > Bachelor | 12 | 14% |
| Researcher | 10 | 11% |
| Student > Master | 10 | 11% |
| Student > Doctoral Student | 6 | 7% |
| Other | 7 | 8% |
| Unknown | 27 | 31% |
| Readers by discipline | Count | As % |
|---|---|---|
| Biochemistry, Genetics and Molecular Biology | 31 | 35% |
| Agricultural and Biological Sciences | 8 | 9% |
| Pharmacology, Toxicology and Pharmaceutical Science | 5 | 6% |
| Medicine and Dentistry | 5 | 6% |
| Chemistry | 3 | 3% |
| Other | 5 | 6% |
| Unknown | 31 | 35% |
Attention Score in Context
This research output has an Altmetric Attention Score of 1. This is our high-level measure of the quality and quantity of online attention that it has received. This Attention Score, as well as the ranking and number of research outputs shown below, was calculated when the research output was last mentioned on 16 March 2018.
All research outputs
#15,495,840
of 23,028,364 outputs
Outputs from Protein & Cell
#481
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Outputs of similar age
#213,366
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Outputs of similar age from Protein & Cell
#16
of 26 outputs
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