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mRNA Interactome Capture from Plant Protoplasts
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RNA Binding by Plant Serpins in vitro.

Eugene A Tolstyko1,2, Denis A Chergintsev3, Olga A Tolicheva2

  • 1Department of Virology, Faculty of Biology, Lomonosov Moscow State University, Moscow, 119234, Russia.

Biochemistry. Biokhimiia
|December 14, 2021
PubMed
Summary

Plant serpins, like Arabidopsis thaliana AtSerpin1, bind to transfer RNA (tRNA). These serpins recognize unique structural motifs in RNA, indicating a role beyond protease inhibition.

Keywords:
RNA bindingRNA structureRNA-binding proteinmicroRNAphloemserpintRNA

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Area of Science:

  • Molecular Biology
  • Plant Biochemistry

Background:

  • Serpins are protease inhibitors found across all life forms.
  • Most plant serpins lack functional characterization, unlike Arabidopsis thaliana AtSerpin1 and Cucurbita maxima CmPS1.
  • CmPS1 is a phloem protein known to bind RNA, particularly tRNA.

Purpose of the Study:

  • To investigate the RNA-binding capabilities of plant serpins.
  • To determine the specificity of interactions between plant serpins and RNA.
  • To elucidate the structural basis for plant serpin-RNA complex formation.

Main Methods:

  • Analysis of tRNA species bound by AtSerpin1 and CmPS1.
  • Testing the binding of CmPS1 to microRNA precursors (pre-miR390) and their mutants.
  • Structural analysis of plant serpin-RNA interactions.

Main Results:

  • Both AtSerpin1 and CmPS1 form complexes with tRNA.
  • Neither serpin exhibited strict selectivity for individual tRNA species.
  • CmPS1 binding to pre-miR390 depends on the presence of unpaired nucleotide residues in the hairpin stem.

Conclusions:

  • Plant serpins interact with structured RNA, not specific RNA sequences.
  • The interaction involves recognition of unique spatial motifs formed by unpaired nucleotides in RNA duplexes.
  • Plant serpins may have roles involving structured RNA recognition beyond protease inhibition.