2L9B

Heterodimer between Rna14p monkeytail domain and Rna15p hinge domain of the yeast CF IA complex

2L9B の概要

• エントリーDOI: 10.2210/pdb2l9b/pdb
• NMR情報: BMRB: 17161
• 分子名称: mRNA 3'-end-processing protein RNA15, mRNA 3'-end-processing protein RNA14 (2 entities in total)
• 機能のキーワード: 3' end mrna maturation, transcription
• 由来する生物種: Saccharomyces cerevisiae (yeast); 詳細
• 細胞内の位置: Nucleus: P25299 P25298
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 18106.66

構造登録者

Moreno-Morcillo, M.,Minvielle-Sebastia, L.,Fribourg, S.,Mackereth, C.D. (登録日: 2011-02-07, 公開日: 2011-04-27, 最終更新日: 2024-05-15)

主引用文献

Moreno-Morcillo, M.,Minvielle-Sebastia, L.,Fribourg, S.,Mackereth, C.D.
Locked Tether Formation by Cooperative Folding of Rna14p Monkeytail and Rna15p Hinge Domains in the Yeast CF IA Complex.
Structure, 19:534-545, 2011

PubMed 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.

PubMed: 21481776
DOI: 10.1016/j.str.2011.02.003

実験手法

SOLUTION NMR