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.

Další údaje

• Originální 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

Anotace

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.

Anotace 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.