ŠTEFL, Richard and Frederic ALLAIN. A novel RNA pentaloop fold involved in targeting ADAR2. RNA. vol. 11, No 5, p. 592-597. ISSN 1355-8382. 2005.
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Basic information
Original name A novel RNA pentaloop fold involved in targeting ADAR2
Name in Czech A novel RNA pentaloop fold involved in targeting ADAR2
Authors ŠTEFL, Richard and Frederic ALLAIN.
Edition RNA, 2005, 1355-8382.
Other information
Original language English
Type of outcome Article in a journal
Field of Study 10600 1.6 Biological sciences
Country of publisher United States of America
Confidentiality degree is not subject to a state or trade secret
Impact factor Impact factor: 6.145
Organization unit Faculty of Science
UT WoS 000228706200006
Keywords in English ADENOSINE DEAMINASES; BACTERIOPHAGE-LAMBDA; CA2+ PERMEABILITY; RECEPTOR CHANNELS; BINDING DOMAIN; RECOGNITION; COMPLEX; ACT; TETRALOOPS;
Tags ACT, ADENOSINE DEAMINASES, BACTERIOPHAGE-LAMBDA, BINDING DOMAIN, CA2+ PERMEABILITY, COMPLEX, RECEPTOR CHANNELS, recognition, TETRALOOPS
Tags International impact, Reviewed
Changed by Changed by: prof. Mgr. Richard Štefl, Ph.D., učo 19362. Changed: 26/1/2007 11:30.
Abstract
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.
Abstract (in Czech)
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.
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