ADAR Proteins: Double-stranded RNA and Z-DNA Binding Domains
Author(s) -
Pierre Barraud,
Frédéric H.T. Allain
Publication year - 2011
Publication title -
current topics in microbiology and immunology
Language(s) - English
Resource type - Book series
SCImago Journal Rank - 0.138
H-Index - 120
eISSN - 2196-9965
pISSN - 0070-217X
DOI - 10.1007/82_2011_145
Subject(s) - adar , rna editing , rna , inosine , rna silencing , biology , rna binding protein , biochemistry , dna , nucleic acid , intron , genetics , adenosine , gene , rna interference
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.
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