A novel RNA pentaloop fold involved in targeting ADAR2

ŠTEFL, Richard a Frederic ALLAIN. A novel RNA pentaloop fold involved in targeting ADAR2. RNA. 2005, roč. 11, č. 5, s. 592-597. ISSN 1355-8382.

Základní údaje

Originální název

A novel RNA pentaloop fold involved in targeting ADAR2

Název česky

A novel RNA pentaloop fold involved in targeting ADAR2

Autoři

ŠTEFL, Richard a Frederic ALLAIN

Vydání

RNA, 2005, 1355-8382

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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: 6.145

Organizační jednotka

Přírodovědecká fakulta

UT WoS

000228706200006

Klíčová slova anglicky

ADENOSINE DEAMINASES; BACTERIOPHAGE-LAMBDA; CA2+ PERMEABILITY; RECEPTOR CHANNELS; BINDING DOMAIN; RECOGNITION; COMPLEX; ACT; TETRALOOPS;

Štítky

ACT, ADENOSINE DEAMINASES, BACTERIOPHAGE-LAMBDA, BINDING DOMAIN, CA2+ PERMEABILITY, COMPLEX, RECEPTOR CHANNELS, recognition, TETRALOOPS

Příznaky

Mezinárodní význam, Recenzováno

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Anotace

V originále

Adenosine deaminases that act on RNA (ADARs) catalyze the site-specific conversion of adenosine to inosine in primary mRNA transcripts, thereby affecting coding potential of mature mRNAs. Structural determinants that define the adenosine moieties for specific ADARs-mediated deaminations are currently unknown. We report the solution structure of the central region of the human R/G stem-loop pre-mRNA, a natural ADAR2 substrate encoding the subunit B of the glutamate receptor (R/G site). The structure reveals that the GCU(A/C)A pentaloop that is conserved in mammals and birds adopts a novel fold. The fold is stabilized by a complex interplay of hydrogen bonds and stacking interactions. We propose that this new pentaloop structure is an important determinant of the R/G site recognition by ADAR2.

Česky

Adenosine deaminases that act on RNA (ADARs) catalyze the site-specific conversion of adenosine to inosine in primary mRNA transcripts, thereby affecting coding potential of mature mRNAs. Structural determinants that define the adenosine moieties for specific ADARs-mediated deaminations are currently unknown. We report the solution structure of the central region of the human R/G stem-loop pre-mRNA, a natural ADAR2 substrate encoding the subunit B of the glutamate receptor (R/G site). The structure reveals that the GCU(A/C)A pentaloop that is conserved in mammals and birds adopts a novel fold. The fold is stabilized by a complex interplay of hydrogen bonds and stacking interactions. We propose that this new pentaloop structure is an important determinant of the R/G site recognition by ADAR2.