| ŠTEFL, Richard, Florian OBERSTRASS, Jeniffer HOOD, Muriel JOURDAN, Michal ZIMMERMANN, Lenka SKŘÍŠOVSKÁ, Christophe MARIS, Li PENG, Ctirad HOFR, Ronald EMESON a Frederic ALLAIN. The Solution Structure of the ADAR2 dsRBM-RNA Complex Reveals a Sequence-Specific Readout of the Minor Groove. CELL. UNITED STATES: CELL PRESS, roč. 143, č. 2, s. 225-237. ISSN 0092-8674. 2010. |
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@article{908019,
author = {Štefl, Richard and Oberstrass, Florian and Hood, Jeniffer and Jourdan, Muriel and Zimmermann, Michal and Skříšovská, Lenka and Maris, Christophe and Peng, Li and Hofr, Ctirad and Emeson, Ronald and Allain, Frederic},
article_location = {UNITED STATES},
article_number = {2},
keywords = {OUBLE-STRANDED-RNA; TORSION ANGLE DYNAMICS; DSRNA-BINDING DOMAIN; ADENOSINE DEAMINASES; RIBONUCLEASE-III; EDITING ENZYME; PROTEIN-KINASE; GLUR-B; NMR; RECOGNITION},
language = {eng},
issn = {0092-8674},
journal = {CELL},
title = {The Solution Structure of the ADAR2 dsRBM-RNA Complex Reveals a Sequence-Specific Readout of the Minor Groove},
volume = {143},
year = {2010}
}
TY - JOUR
ID - 908019
AU - Štefl, Richard - Oberstrass, Florian - Hood, Jeniffer - Jourdan, Muriel - Zimmermann, Michal - Skříšovská, Lenka - Maris, Christophe - Peng, Li - Hofr, Ctirad - Emeson, Ronald - Allain, Frederic
PY - 2010
TI - The Solution Structure of the ADAR2 dsRBM-RNA Complex Reveals a Sequence-Specific Readout of the Minor Groove
JF - CELL
VL - 143
IS - 2
SP - 225-237
EP - 225-237
PB - CELL PRESS
SN - 00928674
KW - OUBLE-STRANDED-RNA
KW - TORSION ANGLE DYNAMICS
KW - DSRNA-BINDING DOMAIN
KW - ADENOSINE DEAMINASES
KW - RIBONUCLEASE-III
KW - EDITING ENZYME
KW - PROTEIN-KINASE
KW - GLUR-B
KW - NMR
KW - RECOGNITION
N2 - 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.
ER -
ŠTEFL, Richard, Florian OBERSTRASS, Jeniffer HOOD, Muriel JOURDAN, Michal ZIMMERMANN, Lenka SKŘÍŠOVSKÁ, Christophe MARIS, Li PENG, Ctirad HOFR, Ronald EMESON a Frederic ALLAIN. The Solution Structure of the ADAR2 dsRBM-RNA Complex Reveals a Sequence-Specific Readout of the Minor Groove. \textit{CELL}. UNITED STATES: CELL PRESS, roč.~143, č.~2, s.~225-237. ISSN~0092-8674. 2010.
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