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

ŠTEFL, Richard, Florian OBERSTRASS, Jeniffer HOOD, Muriel JOURDAN, Michal ZIMMERMANN, Lenka SKŘÍŠOVSKÁ, Christophe MARIS, Li PENG, Ctirad HOFR, Ronald EMESON and 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, 2010, vol. 143, No 2, p. 225-237. ISSN 0092-8674.

Basic information

Original name

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

Name in Czech

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

Authors

ŠTEFL, Richard (203 Czech Republic, guarantor, belonging to the institution), Florian OBERSTRASS (756 Switzerland), Jeniffer HOOD (840 United States of America), Muriel JOURDAN (250 France), Michal ZIMMERMANN (203 Czech Republic, belonging to the institution), Lenka SKŘÍŠOVSKÁ (203 Czech Republic), Christophe MARIS (250 France), Li PENG (840 United States of America), Ctirad HOFR (203 Czech Republic, belonging to the institution), Ronald EMESON (840 United States of America) and Frederic ALLAIN (250 France)

Edition

CELL, UNITED STATES, CELL PRESS, 2010, 0092-8674

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Other information

Language

English

Type of outcome

Článek v odborném periodiku

Field of Study

10600 1.6 Biological sciences

Country of publisher

United States of America

Confidentiality degree

není předmětem státního či obchodního tajemství

Impact factor

Impact factor: 32.406

RIV identification code

RIV/00216224:14310/10:00040623

Organization unit

Faculty of Science

UT WoS

000283052200012

Keywords (in Czech)

OUBLE-STRANDED-RNA; TORSION ANGLE DYNAMICS; DSRNA-BINDING DOMAIN; ADENOSINE DEAMINASES; RIBONUCLEASE-III; EDITING ENZYME; PROTEIN-KINASE; GLUR-B; NMR; RECOGNITION

Keywords in English

OUBLE-STRANDED-RNA; TORSION ANGLE DYNAMICS; DSRNA-BINDING DOMAIN; ADENOSINE DEAMINASES; RIBONUCLEASE-III; EDITING ENZYME; PROTEIN-KINASE; GLUR-B; NMR; RECOGNITION

Tags

Reviewed

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Abstract

V originále

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.

In Czech

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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Links

GAP305/10/1490, research and development project	Name: Strukturní podstata ukončení transkripce nezávislé na poly(A) signálu Investor: Czech Science Foundation
GA204/08/1212, research and development project	Name: Strukturní studium interakcí mezi proteiny a RNA účastnící se v mechanismu kontroly kvality RNA Investor: Czech Science Foundation, Structural studies of protein-RNA complexes involved in RNA quality control
GD204/08/H054, research and development project	Name: Molekulární mechanismy proliferace a diferenciace buněk Investor: Czech Science Foundation, Molecular mechanisms of the cell proliferation and differentiation
IAA401630903, research and development project	Name: Strukturní podstata mechanismu ukončení transkripce nepolyadenylovaných transkriptů Investor: Academy of Sciences of the Czech Republic, Structural basis for transcription termination of nonpolyadenylated transcripts
LA08008, research and development project	Name: Strukturní studium interakcí mezi bíkovinami a poškozenou RNA. Investor: Ministry of Education, Youth and Sports of the CR, Structural studies of protein-RNA complexes involved in RNA quality control
MSM0021622413, plan (intention)	Name: Proteiny v metabolismu a při interakci organismů s prostředím Investor: Ministry of Education, Youth and Sports of the CR, Proteins in metabolism and interaction of organisms with the environment
MSM0021622415, plan (intention)	Name: Molekulární podstata buněčných a tkáňových regulací Investor: Ministry of Education, Youth and Sports of the CR, Molecular basis of cell and tissue regulations