5F5F

X-ray structure of Roquin ROQ domain in complex with a Selex-derived hexa-loop RNA motif

Summary for 5F5F

• Entry DOI: 10.2210/pdb5f5f/pdb
• Descriptor: Roquin-1, RNA (5'-R(P*UP*GP*AP*CP*UP*GP*CP*GP*UP*UP*UP*UP*AP*GP*GP*AP*GP*UP*UP*A)-3') (3 entities in total)
• Functional Keywords: roq domain, winged-helix domain, rna binding protein, selex
• Biological source: Mus musculus (House mouse); More
• Total number of polymer chains: 8
• Total formula weight: 111826.04

Authors

Janowski, R.,Schlundt, A.,Sattler, M.,Niessing, D. (deposition date: 2015-12-04, release date: 2016-04-06, Last modification date: 2024-01-10)

Primary citation

Janowski, R.,Heinz, G.A.,Schlundt, A.,Wommelsdorf, N.,Brenner, S.,Gruber, A.R.,Blank, M.,Buch, T.,Buhmann, R.,Zavolan, M.,Niessing, D.,Heissmeyer, V.,Sattler, M.
Roquin recognizes a non-canonical hexaloop structure in the 3'-UTR of Ox40.
Nat Commun, 7:11032-11032, 2016

PubMed Abstract: The RNA-binding protein Roquin is required to prevent autoimmunity. Roquin controls T-helper cell activation and differentiation by limiting the induced expression of costimulatory receptors such as tumor necrosis factor receptor superfamily 4 (Tnfrs4 or Ox40). A constitutive decay element (CDE) with a characteristic triloop hairpin was previously shown to be recognized by Roquin. Here we use SELEX assays to identify a novel U-rich hexaloop motif, representing an alternative decay element (ADE). Crystal structures and NMR data show that the Roquin-1 ROQ domain recognizes hexaloops in the SELEX-derived ADE and in an ADE-like variant present in the Ox40 3'-UTR with identical binding modes. In cells, ADE-like and CDE-like motifs cooperate in the repression of Ox40 by Roquin. Our data reveal an unexpected recognition of hexaloop cis elements for the posttranscriptional regulation of target messenger RNAs by Roquin.

PubMed: 27010430
DOI: 10.1038/ncomms11032

Experimental method

X-RAY DIFFRACTION (3 Å)