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RNA-binding proteins that preferentially interact with 8-oxoG-modified RNAs: our current understanding.

Kathleen E Taylor1, Lucas G Miller1, Lydia M Contreras1,2

  • 1McKetta Department of Chemical Engineering, University of Texas at Austin, Austin, TX, USA.

Biochemical Society Transactions
|January 4, 2024
PubMed
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Oxidative stress damages RNA, creating 8-oxo-7,8-hydroxyguanine (8-oxoG). Four proteins, including polynucleotide phosphorylase (PNPase), bind this modified RNA, aiding cell survival under stress.

Keywords:
RNA modificationsRNA-binding proteinsepitranscriptomicsoxidative stress

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Area of Science:

  • Molecular Biology
  • Cellular Stress Response
  • RNA Biology

Background:

  • Cells face oxidative stress from toxins and UV light, causing RNA modifications.
  • Oxidized guanine (8-oxoG) disrupts RNA translation and stability.
  • This modification is a key factor in cellular damage and dysfunction.

Conclusions:

  • PNPase, HNRPD/Auf1, PCBP1, and YB-1 are key players in the cellular response to oxidative stress.
  • Their ability to bind 8-oxoG-modified RNA is critical for maintaining cellular integrity.
  • Further research into these proteins may reveal therapeutic targets for oxidative stress-related diseases.