Structure and specific RNA-binding of ADAR2 double-stranded RNA-binding motifs
Identifikátory výsledku
Kód výsledku v IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F06%3A00018575" target="_blank" >RIV/00216224:14310/06:00018575 - isvavai.cz</a>
Výsledek na webu
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DOI - Digital Object Identifier
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Alternativní jazyky
Jazyk výsledku
angličtina
Název v původním jazyce
Structure and specific RNA-binding of ADAR2 double-stranded RNA-binding motifs
Popis výsledku v původním jazyce
Adenosine deaminases that act on RNA (ADARs) tune and regulate gene expression. Although ADARs act mostly as nonspecific enzymes, they can recode certain genes in a highly specific manner. This results from preferential binding of the ADARs to certain RNA substrates. To understand how ADARs bind RNA, we investigated the N-terminal region of ADAR2 by nuclear magnetic resonance (NMR) spectroscopy. This region is responsible for RNA binding and consists of the two double-stranded RNA-binding motifs (dsRBMs). We determined the structure of these two dsRBMs and carried out an NMR chemical shift perturbation study of the interaction of the two dsRBMs with a 71 nucleotide RNA encoding the R/G site of the GluR-B. Based on our precise identification of both theprotein and RNA interaction surfaces, we built an NMR-derived model of the ADAR2 dsRBMs in complex with the R/G stem-loop RNA. We showed that each dsRBM binds a different structural element of the R/G stem-loop; dsRBM1 binds a stem cappe
Název v anglickém jazyce
Structure and specific RNA-binding of ADAR2 double-stranded RNA-binding motifs
Popis výsledku anglicky
Adenosine deaminases that act on RNA (ADARs) tune and regulate gene expression. Although ADARs act mostly as nonspecific enzymes, they can recode certain genes in a highly specific manner. This results from preferential binding of the ADARs to certain RNA substrates. To understand how ADARs bind RNA, we investigated the N-terminal region of ADAR2 by nuclear magnetic resonance (NMR) spectroscopy. This region is responsible for RNA binding and consists of the two double-stranded RNA-binding motifs (dsRBMs). We determined the structure of these two dsRBMs and carried out an NMR chemical shift perturbation study of the interaction of the two dsRBMs with a 71 nucleotide RNA encoding the R/G site of the GluR-B. Based on our precise identification of both theprotein and RNA interaction surfaces, we built an NMR-derived model of the ADAR2 dsRBMs in complex with the R/G stem-loop RNA. We showed that each dsRBM binds a different structural element of the R/G stem-loop; dsRBM1 binds a stem cappe
Klasifikace
Druh
A - Audiovizuální tvorba
CEP obor
CE - Biochemie
OECD FORD obor
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Návaznosti výsledku
Projekt
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Návaznosti
Z - Vyzkumny zamer (s odkazem do CEZ)
Ostatní
Rok uplatnění
2006
Kód důvěrnosti údajů
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Údaje specifické pro druh výsledku
ISBN
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Místo vydání
Brno
Název nakladatele resp. objednatele
Masaryk University
Verze
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Identifikační číslo nosiče
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