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The G4 resolvase RHAU modulates mRNA translation and stability to sustain postnatal heart function and regeneration.

Authors
  • Jiang, Mingyang1
  • Hu, Han2
  • Zhao, Ke1
  • Di, Ruomin3
  • Huang, Xinyi1
  • Shi, Yingchao1
  • Yue, Yunyun1
  • Nie, Junwei1
  • Yu, Shan1
  • Wang, Wengong4
  • Yang, Zhongzhou5
  • 1 Nanjing University, China. , (China)
  • 2 Peking University Health Science Center,, China. , (China)
  • 3 The Fifth People's Hospital of Shanghai, China. , (China)
  • 4 Peking University Health Science Center, China. , (China)
  • 5 Medical School, Nanjing University, China. , (China)
Type
Published Article
Journal
Journal of Biological Chemistry
Publisher
American Society for Biochemistry and Molecular Biology
Publication Date
Nov 16, 2020
Identifiers
DOI: 10.1074/jbc.RA120.014948
PMID: 33199370
Source
Medline
Keywords
Language
English
License
Unknown

Abstract

Post-transcriptional regulation of mRNA translation and stability is primarily achieved by RNA binding proteins (RBPs), which is of increasing importance for heart function. Furthermore, G-quadruplex (G4) and G4 resolvase activity are involved in a variety of biological processes. However, the role of G4 resolvase activity in heart function remains unknown. The present study aims to investigate the role of RHAU, an RBP with G4 resolvase activity in postnatal heart function through deletion of Rhau in the cardiomyocytes of postnatal mice. RHAU-deficient mice displayed progressive pathological remodeling leading to heart failure and mortality, and impaired neonatal heart regeneration. RHAU ablation reduced the protein levels but enhanced mRNA levels of Yap1 and Hexim1 that are important regulators for heart development and postnatal heart function. Furthermore, RHAU was found to associate with both the 5'- and 3'- UTRs of these genes to destabilize mRNA but to enhance translation. Thus, we have demonstrated the important functions of RHAU in the dual regulation of mRNA translation and stability, which is vital for heart physiology. Published under license by The American Society for Biochemistry and Molecular Biology, Inc.

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