ADAR Proteins: Double-stranded RNA and Z-DNA Binding Domains

被引:66
|
作者
Barraud, Pierre [1 ]
Allain, Frederic H. -T. [1 ]
机构
[1] ETH, Inst Mol Biol & Biophys, CH-8093 Zurich, Switzerland
来源
ADENOSINE DEAMINASES ACTING ON RNA (ADARS) AND A-TO-I EDITING | 2012年 / 353卷
关键词
EDITING ENZYME ADAR1; Z-ALPHA DOMAIN; DSRNA-ADENOSINE-DEAMINASE; B-Z TRANSITION; HANDED Z-DNA; UNWINDING ACTIVITY; CRYSTAL-STRUCTURE; INTERFERON ACTION; MEASLES-VIRUS; EXPORT SIGNAL;
D O I
10.1007/82_2011_145
中图分类号
R392 [医学免疫学]; Q939.91 [免疫学];
学科分类号
100102 ;
摘要
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.
引用
收藏
页码:35 / 60
页数:26
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