Unknown

Dataset Information

0

ADAR proteins: double-stranded RNA and Z-DNA binding domains.


ABSTRACT: Adenosine deaminases acting on RNA (ADAR) catalyze adenosine to inosine editing within double-stranded RNA (dsRNA) substrates. Inosine is read as a guanine by most cellular processes and therefore these changes create codons for a different amino acid, stop codons or even a new splice-site allowing protein diversity generated from a single gene. We review here the current structural and molecular knowledge on RNA editing by the ADAR family of protein. We focus especially on two types of nucleic acid binding domains present in ADARs, namely the dsRNA and Z-DNA binding domains.

SUBMITTER: Barraud P 

PROVIDER: S-EPMC3226063 | biostudies-literature | 2012

REPOSITORIES: biostudies-literature

altmetric image

Publications

ADAR proteins: double-stranded RNA and Z-DNA binding domains.

Barraud Pierre P   Allain Frédéric H-T FH  

Current topics in microbiology and immunology 20120101


Adenosine deaminases acting on RNA (ADAR) catalyze adenosine to inosine editing within double-stranded RNA (dsRNA) substrates. Inosine is read as a guanine by most cellular processes and therefore these changes create codons for a different amino acid, stop codons or even a new splice-site allowing protein diversity generated from a single gene. We review here the current structural and molecular knowledge on RNA editing by the ADAR family of protein. We focus especially on two types of nucleic  ...[more]

Similar Datasets

| S-EPMC3113232 | biostudies-literature
| S-EPMC4551942 | biostudies-literature
| S-EPMC4615638 | biostudies-literature
| S-EPMC5587031 | biostudies-literature
| S-EPMC3538233 | biostudies-literature
| S-EPMC3816740 | biostudies-literature
| S-EPMC5852647 | biostudies-literature
| S-EPMC3724394 | biostudies-literature