2010
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 et. al.Základní údaje
Originální název
The Solution Structure of the ADAR2 dsRBM-RNA Complex Reveals a Sequence-Specific Readout of the Minor Groove
Název česky
The Solution Structure of the ADAR2 dsRBM-RNA Complex Reveals a Sequence-Specific Readout of the Minor Groove
Autoři
ŠTEFL, Richard (203 Česká republika, garant, domácí), Florian OBERSTRASS (756 Švýcarsko), Jeniffer HOOD (840 Spojené státy), Muriel JOURDAN (250 Francie), Michal ZIMMERMANN (203 Česká republika, domácí), Lenka SKŘÍŠOVSKÁ (203 Česká republika), Christophe MARIS (250 Francie), Li PENG (840 Spojené státy), Ctirad HOFR (203 Česká republika, domácí), Ronald EMESON (840 Spojené státy) a Frederic ALLAIN (250 Francie)
Vydání
CELL, UNITED STATES, CELL PRESS, 2010, 0092-8674
Další údaje
Jazyk
angličtina
Typ výsledku
Článek v odborném periodiku
Obor
10600 1.6 Biological sciences
Stát vydavatele
Spojené státy
Utajení
není předmětem státního či obchodního tajemství
Impakt faktor
Impact factor: 32.406
Kód RIV
RIV/00216224:14310/10:00040623
Organizační jednotka
Přírodovědecká fakulta
UT WoS
000283052200012
Klíčová slova česky
OUBLE-STRANDED-RNA; TORSION ANGLE DYNAMICS; DSRNA-BINDING DOMAIN; ADENOSINE DEAMINASES; RIBONUCLEASE-III; EDITING ENZYME; PROTEIN-KINASE; GLUR-B; NMR; RECOGNITION
Klíčová slova anglicky
OUBLE-STRANDED-RNA; TORSION ANGLE DYNAMICS; DSRNA-BINDING DOMAIN; ADENOSINE DEAMINASES; RIBONUCLEASE-III; EDITING ENZYME; PROTEIN-KINASE; GLUR-B; NMR; RECOGNITION
Příznaky
Recenzováno
Změněno: 14. 12. 2010 16:41, doc. Mgr. Ctirad Hofr, Ph.D.
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.
Česky
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.
Návaznosti
| GAP305/10/1490, projekt VaV |
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| GA204/08/1212, projekt VaV |
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| GD204/08/H054, projekt VaV |
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| IAA401630903, projekt VaV |
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| LA08008, projekt VaV |
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| MSM0021622413, záměr |
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| MSM0021622415, záměr |
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