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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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Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
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Base complementarity between the three base pairs of mRNA codon and the tRNA anticodon is not a failsafe mechanism. Inaccuracies can range from a single mismatch to no correct base pairing at all. The free energy difference between the correct and nearly correct base pairs can be as small as 3 kcal/ mol. With complementarity being the only proofreading step, the estimated error frequency would be one wrong amino acid in every 100 amino acids incorporated. However, error frequencies observed in...
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A Nonsequencing Approach for the Rapid Detection of RNA Editing
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Stereoretentive Post-Translational Protein Editing.

Xia-Ping Fu1,2, Yizhi Yuan1,2, Ajay Jha1,2

  • 1Rosalind Franklin Institute, Harwell, Oxfordshire OX11 0QX, United Kingdom.

ACS Central Science
|March 27, 2023
PubMed
Summary
This summary is machine-generated.

This study introduces a novel light-mediated method for protein side-chain editing. It enables the creation of diverse, stereochemically pure modified proteins from natural amino acid precursors without genetic manipulation.

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Area of Science:

  • Biochemistry
  • Chemical Biology
  • Synthetic Biology

Background:

  • Chemical post-translational methods offer protein editing without genetic intervention.
  • Current C-C bond forming methods often yield undesired epimeric mixtures.

Purpose of the Study:

  • To develop a stereoselective method for protein side-chain modification.
  • To enable the formation of new C-C, C-H, C-O, C-Se, and C-B bonds on proteins.

Main Methods:

  • Light-mediated desulfurative reaction of on-protein l-alanyl radicals.
  • Utilizing a natural amino acid precursor for modification.

Main Results:

  • Achieved stereoretention during radical formation and reaction.
  • Demonstrated formation of diverse C-C, C-H, C-O, C-Se, and C-B bonds.
  • Generated site-selectively edited proteins with native stereochemistry.

Conclusions:

  • The developed method allows flexible protein side-chain editing with high stereochemical control.
  • This approach expands possibilities for exploring protein function and creating bioconjugates.