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RNA editing is a post-transcriptional modification where a precursor mRNA (pre-mRNA) nucleotide sequence is changed by base insertion, deletion, or modification. The extent of RNA editing varies from a few hundred bases, in mitochondrial DNA of trypanosomes, to a just single base, in nuclear genes of mammals. Even a single base change in the pre-mRNA can convert a codon for one amino acid into the codon for another amino acid or a stop codon. This type of re-coding can significantly affect the...
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Intact DNA strands can be found in fossils, while scientists sometimes struggle to keep RNA intact under laboratory conditions. The structural variations between RNA and DNA underlie the differences in their stability and longevity. Because DNA is double-stranded, it is inherently more stable. The single-stranded structure of RNA is less stable but also more flexible and can form weak internal bonds. Additionally, most RNAs in the cell are relatively short, while DNA can be up to 250 million...
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One of the unique features of tRNA is the presence of modified bases. In some tRNAs, modified bases account for nearly 20% of the total bases in the molecule. Altogether, these unusual bases protect the tRNA from enzymatic degradation by RNases.
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The basic structure of RNA consists of a five-carbon sugar and one of four nitrogenous bases. Although most RNA is single-stranded, it can form complex secondary and tertiary structures. Such structures play essential roles in the regulation of transcription and translation.
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Related Experiment Video

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Extremely Rapid and Specific Metabolic Labelling of RNA In Vivo with 4-Thiouracil Ers4tU
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Reversible RNA ADP-ribosylation on uracil bases.

Yang Lu1, Li Tang2,3,4, Øyvind Strømland5

  • 1Sir William Dunn School of Pathology, University of Oxford, OxfordOX1 3RE, United Kingdom.

Nucleic Acids Research
|March 31, 2026
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Human PARP10 modifies nucleic acid bases, and TARG1 proteins reverse uracil base ADP-ribosylation (U-ADPr). This suggests U-ADPr is an evolutionarily conserved biological signal across species.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Genetics

Background:

  • ADP-ribosylation regulates cellular processes like genome stability.
  • While protein ADP-ribosylation is well-studied, nucleic acid ADP-ribosylation is less understood in higher organisms.
  • Poly(ADP-ribose) Polymerases (PARPs) are key enzymes in human ADP-ribosylation.

Purpose of the Study:

  • To identify enzymes involved in nucleic acid base ADP-ribosylation in humans.
  • To characterize the enzymes responsible for reversing uracil base ADP-ribosylation (U-ADPr).
  • To investigate the evolutionary conservation of U-ADPr reversal.

Main Methods:

  • Enzyme activity assays using human PARP10 and TARG1.
  • Development of chemical probes for U-ADPr characterization.
  • Comparative analysis of U-ADPr hydrolases in humans, Drosophila, and bacteria.

Main Results:

  • Human PARP10 was identified as an enzyme that ADP-ribosylates uracil bases in RNA and thymine bases in DNA.
  • Human TARG1 efficiently reverses U-ADPr.
  • TARG1 and TARG1-like proteins were confirmed as efficient U-ADPr hydrolases across different species.

Conclusions:

  • PARP10 plays a role in nucleic acid base ADP-ribosylation.
  • TARG1 and related proteins are crucial for U-ADPr reversal in humans and other organisms.
  • The findings suggest U-ADPr is a conserved biological signal with evolutionary significance.