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Updated: Jan 1, 2026

Sample Preparation for Mass Spectrometry-based Identification of RNA-binding Regions
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Structural basis for mRNA recognition by human RBM38

Kaiyue Qian1,2,3, Mengyu Li1,3, Junchao Wang1,2,3

  • 1School of Life Sciences, Anhui University, Hefei, Anhui 230601, China.

The Biochemical Journal
|December 21, 2019
PubMed

Insights

The RNA-binding protein RBM38 recognizes specific RNA sequences via its RRM domain. Structural analysis reveals key interactions, clarifying how RBM38 binds RNA.

Area of Science:

  • Molecular Biology
  • Structural Biology
  • Genetics

Background:

  • RNA-binding protein RBM38 interacts with p53-related gene mRNAs.
  • RBM38 influences protein translation through mRNA stability and effector recruitment.
  • The precise RNA recognition mechanism of RBM38 is not fully understood.

Purpose of the Study:

  • To elucidate the RNA recognition mechanism of the RBM38 RNA-recognition motif (RRM) domain.
  • To determine the structural basis for RBM38's sequence-specific RNA binding.

Main Methods:

  • X-ray crystallography was used to determine the structure of the RBM38 RRM domain in complex with single-stranded RNA.
  • Structural and biological analyses were performed to identify key binding interactions.

Main Results:

  • The crystal structure of the human RBM38 RRM domain bound to single-stranded RNA was determined.
  • RBM38 specifically recognizes the RNA sequence G(U/C/A)GUG.
  • Two phenylalanine residues are critical for RNA binding through base stacking.
  • Hydrogen bonds between RBM38 and RNA bases mediate sequence-specific recognition.

Conclusions:

  • The study reveals the sequence- and structure-specific RNA recognition mechanism of human RBM38.
  • Structural insights are provided for understanding RBM38's RNA-binding properties and functions.
Keywords:
RBM38RNARNA-binding proteinscrystallographytranslational regulation

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