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Updated: May 6, 2026

Sequence-specific and Selective Recognition of Double-stranded RNAs over Single-stranded RNAs by Chemically Modified Peptide Nucleic Acids
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Structural basis for RNA recognition by a dimeric PPR-protein complex.

Jiyuan Ke1, Run-Ze Chen, Ting Ban

  • 11] Laboratory of Structural Sciences, Center for Structural Biology and Drug Discovery, Van Andel Research Institute, Grand Rapids, Michigan, USA. [2].

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|November 5, 2013
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Summary
This summary is machine-generated.

Thylakoid assembly 8 (THA8) protein binds ycf3 intron RNA, inducing dimer formation. This RNA-induced dimerization reveals a novel mechanism for PPR protein RNA recognition in chloroplast development.

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Area of Science:

  • Chloroplast biology
  • RNA-protein interactions
  • Molecular mechanisms of gene expression

Background:

  • Thylakoid assembly 8 (THA8) is a pentatricopeptide repeat (PPR) protein crucial for ycf3 transcript splicing.
  • Ycf3 is essential for chloroplast thylakoid-membrane biogenesis.

Purpose of the Study:

  • To identify THA8-binding sites within the ycf3 intron.
  • To elucidate the structural basis of THA8-RNA interaction and RNA recognition mechanism.

Main Methods:

  • Identification of THA8-binding sites in the ycf3 intron.
  • X-ray crystallography of Brachypodium distachyon THA8 (apo and RNA-bound states).

Main Results:

  • Multiple THA8-binding sites were identified in the ycf3 intron.
  • Crystal structures revealed THA8 monomers with five PPR repeats.
  • RNA binding induced the formation of asymmetric THA8 dimers, with RNA at the dimeric interface.
  • A conserved guanine nucleotide in the RNA forms extensive contacts within the dimer.

Conclusions:

  • A novel model for RNA recognition by PPR proteins is proposed, involving RNA-induced asymmetric dimer formation.
  • This mechanism highlights a new mode of RNA binding mediated by PPR proteins in chloroplast gene expression.