2X1F

Structure of Rna15 RRM with bound RNA (GU)

Summary for 2X1F

• Entry DOI: 10.2210/pdb2x1f/pdb
• Related: 2X1A 2X1B
• Descriptor: MRNA 3'-END-PROCESSING PROTEIN RNA15, 5'-R(*GP*UP*UP*GP*UP)-3' (3 entities in total)
• Functional Keywords: transcription-rna complex, mrna processing, transcription/rna
• Biological source: SACCHAROMYCES CEREVISIAE (BAKER'S YEAST)
• Total number of polymer chains: 2
• Total formula weight: 12332.95

Authors

Pancevac, C.,Goldstone, D.C.,Ramos, A.,Taylor, I.A. (deposition date: 2010-01-06, release date: 2010-02-02, Last modification date: 2024-05-08)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.6 Å)