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The Solution Structure of the ADAR2 dsRBM-RNA Complex Reveals a Sequence-Specific Readout of the Minor Groove

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ŠTEFL Richard OBERSTRASS Florian HOOD Jeniffer JOURDAN Muriel ZIMMERMANN Michal SKŘÍŠOVSKÁ Lenka MARIS Christophe PENG Li HOFR Ctirad EMESON Ronald ALLAIN Frederic

Rok publikování 2010
Druh Článek v odborném periodiku
Časopis / Zdroj CELL
Fakulta / Pracoviště MU

Přírodovědecká fakulta

Citace
Obor Biochemie
Klíčová slova OUBLE-STRANDED-RNA; TORSION ANGLE DYNAMICS; DSRNA-BINDING DOMAIN; ADENOSINE DEAMINASES; RIBONUCLEASE-III; EDITING ENZYME; PROTEIN-KINASE; GLUR-B; NMR; RECOGNITION
Popis Sequence-dependent recognition of dsDNA-binding proteins is well understood, yet sequence-specific recognition of dsRNA by proteins remains largely unknown, despite their importance in RNA maturation pathways. Adenosine deaminases that act on RNA (ADARs) recode genomic information by the site-selective deamination of adenosine. Here, we report the solution structure of the ADAR2 double-stranded RNA-binding motifs (dsRBMs) bound to a stem-loop pre-mRNA encoding the R/G editing site of GluR-2. The structure provides a molecular basis for how dsRBMs recognize the shape, and also more surprisingly, the sequence of the dsRNA. The unexpected direct readout of the RNA primary sequence by dsRBMs is achieved via the minor groove of the dsRNA and this recognition is critical for both editing and binding affinity at the R/G site of GluR-2. More generally, our findings suggest a solution to the sequence-specific paradox faced by many dsRBM-containing proteins that are involved in post-transcriptional regulation of gene expression.
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