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Updated: Oct 10, 2025

DNAzyme-dependent Analysis of rRNA 2’-O-Methylation
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Recognition of G-quadruplex RNA by a crucial RNA methyltransferase component, METTL14

Atsuhiro Yoshida1, Takanori Oyoshi2, Akiyo Suda1

  • 1Institute for Chemical Research, Kyoto University, Uji, Kyoto 611-0011, Japan.

Nucleic Acids Research
|December 15, 2021
PubMed

Insights

The METTL3/METTL14 enzyme complex preferentially binds RNA G-quadruplex (rG4) structures. This binding preference guides the N6-methyladenosine (m6A) modification to specific sites near these structures.

Area of Science:

  • Molecular Biology
  • Epigenetics
  • RNA Biology

Background:

  • N6-methyladenosine (m6A) is a crucial epitranscriptomic modification.
  • The METTL3/METTL14 complex catalyzes m6A methylation.
  • The precise RNA targeting mechanism of METTL3/METTL14 remains unclear.

Purpose of the Study:

  • To elucidate the RNA binding properties of the METTL3/METTL14 complex.
  • To understand how METTL3/METTL14 selects its target RNAs.

Main Methods:

  • Investigated RNA binding preferences of the METTL3/METTL14 heterodimer.
  • Assessed methylation activity near specific RNA structures.

Main Results:

  • The METTL3/METTL14 complex exhibits a binding preference for RNA G-quadruplex (rG4) structures.
  • Binding occurs via the METTL14 RGG repeats.
  • Methylation is selectively targeted to adenosines adjacent to rG4 sequences.

Conclusions:

  • RNA G-quadruplex structures may directly recruit the METTL3/METTL14 complex.
  • This study reveals a novel role for rG4 structures in guiding m6A epitranscriptomic regulation.
  • Provides insights into the specificity of the m6A writer complex.

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