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Locked tether formation by cooperative folding of Rna14p monkeytail and Rna15p hinge domains in the yeast CF IA

Maria Moreno-Morcillo1, Lionel Minvielle-Sébastia, Sébastien Fribourg

  • 1Institut Européen de Chimie et Biologie and INSERM U869, 33607 Pessac Cedex, France.

Structure (London, England : 1993)
|April 13, 2011
PubMed

Insights

Researchers studied the yeast CF IA complex, crucial for mRNA maturation. They revealed how Rna14p and Rna15p proteins interact, a mechanism conserved in mammals.

Area of Science:

  • Molecular Biology
  • Biochemistry
  • Genetics

Background:

  • mRNA maturation involves pre-mRNA 3' end processing, including cleavage and polyadenylation.
  • The cleavage/polyadenylation factor IA (CF IA) complex in Saccharomyces cerevisiae is essential for this process.
  • CF IA comprises four proteins (Clp1p, Pcf11p, Rna14p, Rna15p) that recognize RNA sequences and recruit other factors.

Purpose of the Study:

  • To elucidate the molecular architecture of the CF IA complex.
  • To understand the interaction between Rna14p and Rna15p within CF IA.
  • To investigate the mechanism of their coupled binding and folding.

Main Methods:

  • Solution structure determination of the Rna14p-Rna15p heterodimer.
  • Analysis of protein-protein interactions within the CF IA complex.
  • Site-directed mutagenesis to study the role of specific domains and interactions.

Main Results:

  • The study solved the solution structure of the interacting regions between Rna14p and Rna15p.
  • A coupled binding and folding mechanism was identified for the Rna14p monkeytail and Rna15p hinge regions.
  • Destabilizing mutations in this interaction prevent Rna15p association within CF IA.
  • Conserved residues indicate similar structural tethering in mammalian CstF-77 and CstF-64 proteins.

Conclusions:

  • The Rna14p-Rna15p interaction is critical for CF IA assembly and function in yeast.
  • This structural mechanism is conserved across species, highlighting its fundamental importance in mRNA processing.
  • Understanding this interaction provides insights into mRNA 3' end formation regulation.

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