2X1B

Structure of RNA15 RRM

2X1B の概要

• エントリーDOI: 10.2210/pdb2x1b/pdb
• 関連するPDBエントリー: 2X1A 2X1F
• 分子名称: MRNA 3'-END-PROCESSING PROTEIN RNA15, PHOSPHATE ION (3 entities in total)
• 機能のキーワード: transcription, nucleus, rna-binding, mrna processing
• 由来する生物種: SACCHAROMYCES CEREVISIAE (BAKER'S YEAST)
• 細胞内の位置: Nucleus: P25299
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 10895.92

構造登録者

Pancevac, C.,Goldstone, D.C.,Ramos, A.,Taylor, I.A. (登録日: 2010-01-06, 公開日: 2010-02-02, 最終更新日: 2024-05-08)

主引用文献

Pancevac, C.,Goldstone, D.C.,Ramos, A.,Taylor, I.A.
Structure of the RNA15 Rrm-RNA Complex Reveals the Molecular Basis of Gu Specificity in Transcriptional 3-End Processing Factors.
Nucleic Acids Res., 38:3119-, 2010

PubMed Abstract: Rna15 is a core subunit of cleavage factor IA (CFIA), an essential transcriptional 3'-end processing factor from Saccharomyces cerevisiae. CFIA is required for polyA site selection/cleavage targeting RNA sequences that surround polyadenylation sites in the 3'-UTR of RNA polymerase-II transcripts. RNA recognition by CFIA is mediated by an RNA recognition motif (RRM) contained in the Rna15 subunit of the complex. We show here that Rna15 has a strong and unexpected preference for GU containing RNAs and reveal the molecular basis for a base selectivity mechanism that accommodates G or U but discriminates against C and A bases. This mode of base selectivity is rather different to that observed in other RRM-RNA structures and is structurally conserved in CstF64, the mammalian counterpart of Rna15. Our observations provide evidence for a highly conserved mechanism of base recognition amongst the 3'-end processing complexes that interact with the U-rich or U/G-rich elements at 3'-end cleavage/polyadenylation sites.

PubMed: 20097654
DOI: 10.1093/NAR/GKQ002

実験手法

X-RAY DIFFRACTION (1.8 Å)