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Tumor suppressor RBM5 directly interacts with the DExD/H-box protein DHX15 and stimulates its helicase activity

Zhaoyang Niu1, Wenxing Jin, Libo Zhang

  • 1Graduate Program in Chinese Academy of Medical Sciences and Peking Union Medical College, Beijing 100730, China.

FEBS Letters
|May 10, 2012
PubMed

Insights

RNA binding motif protein 5 (RBM5) regulates pre-mRNA splicing by interacting with spliceosome components DHX15 and PRP19. RBM5

Area of Science:

  • Molecular Biology
  • RNA Splicing
  • Gene Regulation

Background:

  • RNA binding motif protein 5 (RBM5) is implicated as a tumor suppressor.
  • RBM5 is known to regulate alternative splicing of apoptosis-related genes.

Purpose of the Study:

  • To identify novel RBM5-interacting partners.
  • To elucidate the mechanism by which RBM5 regulates pre-mRNA splicing.

Main Methods:

  • Co-immunoprecipitation assays to identify RBM5-interacting proteins.
  • In vitro helicase activity assays to assess the functional interaction between RBM5 and DHX15.
  • Site-directed mutagenesis to investigate the role of the RBM5 G-patch domain.

Main Results:

  • DHX15 and PRP19 were identified as novel RBM5-interacting partners.
  • The G-patch domain of RBM5 is essential for its interaction with DHX15.
  • RBM5 enhances the helicase activity of DHX15 in vitro, dependent on its G-patch domain.

Conclusions:

  • RBM5 interacts with spliceosome components DHX15 and PRP19.
  • RBM5 modulates DHX15 helicase activity, suggesting a novel mechanism for RBM5's role in pre-mRNA splicing regulation.

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