2l9b Citations

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

Abstract

The removal of the 3' region of pre-mRNA followed by polyadenylation is a key step in mRNA maturation. In the yeast Saccharomyces cerevisiae, one component of the processing machinery is the cleavage/polyadenylation factor IA (CF IA) complex, composed of four proteins (Clp1p, Pcf11p, Rna14p, Rna15p) that recognize RNA sequences adjacent to the cleavage site and recruit additional processing factors. To gain insight into the molecular architecture of CF IA we solved the solution structure of the heterodimer composed of the interacting regions between Rna14p and Rna15p. The C-terminal monkeytail domain from Rna14p and the hinge region from Rna15p display a coupled binding and folding mechanism, where both peptides are initially disordered. Mutants with destabilized monkeytail-hinge interactions prevent association of Rna15p within CF IA. Conservation of interdomain residues reveals that the structural tethering is preserved in the homologous mammalian cleavage stimulation factor (CstF)-77 and CstF-64 proteins of the CstF complex.

Reviews - 2l9b mentioned but not cited (1)

  1. Delineating the structural blueprint of the pre-mRNA 3'-end processing machinery. Xiang K, Tong L, Manley JL. Mol Cell Biol 34 1894-1910 (2014)

Articles - 2l9b mentioned but not cited (5)



Reviews citing this publication (3)

  1. Recent molecular insights into canonical pre-mRNA 3'-end processing. Sun Y, Hamilton K, Tong L. Transcription 11 83-96 (2020)
  2. Alternative polyadenylation of mRNA and its role in cancer. Yuan F, Hankey W, Wagner EJ, Li W, Wang Q. Genes Dis 8 61-72 (2021)
  3. The long and the short of it: the role of the zinc finger polyadenosine RNA binding protein, Nab2, in control of poly(A) tail length. Soucek S, Corbett AH, Fasken MB. Biochim Biophys Acta 1819 546-554 (2012)

Articles citing this publication (11)