By Rena A. Goodman, Mark R. Macbeth (auth.), Charles E. Samuel (eds.)

ISBN-10: 3642228003

ISBN-13: 9783642228001

“The aim of this CTMI quantity is to supply readers with a starting place for realizing what ADARs are and the way they act to impact gene expression and serve as. it truly is changing into more and more obvious that ADARs may perhaps own roles not just as enzymes that deaminate adenosine to provide inosine in RNA substrates with double-stranded personality, but in addition as proteins self sustaining in their catalytic estate. simply because A-to-I modifying may possibly have an effect on base-pairing and RNA constitution, approaches together with translation, splicing, RNA replication, and miR and siRNA silencing could be affected. destiny experiences of ADARs doubtless will supply us with extra surprises and new insights into the modulation of organic techniques by means of the ADAR family members of proteins.”

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Instead, they chose to make a mutation in a conserved KKXXK stretch that is known to be involved in RNA binding in other dsRNA binding proteins. This mutation disrupted RNA binding but in fact still allowed observation of protein dimerization. The authors observed that a dimer in which only one unit was 26 R. A. Goodman et al. able to bind RNA was not catalytically active, whereas a dimer in which both units were able to bind RNA but only one of the units was catalytically active still exhibited 50% activity.

Interestingly, a recent study showed that an R-domain is also present in a minor splicing variant of ADAR2 (Maas and Gommans 2009). After the presentation of ADARs editing substrates, the structure and function of the Z-DNA binding domains and the dsRNA binding domains of ADAR will be described in the remaining sections. 1 Specificity of Editing Adenosine deaminases that act on RNA (ADARs) convert adenosine into inosine in cellular and viral RNA transcripts containing either perfect or imperfect regions of double-stranded RNA (dsRNA) (Gott and Emeson 2000; Bass 2002; Nishikura 2010).

2006). However, the observations that dsRBM1 is required for binding whereas dsRBM2 is required for catalytic activity are hard to reconcile, considering that RNA binding is necessary for robust catalytic activity (Macbeth et al. 2005). Valente et al. suggest that this may be explained by the choice of mutation made to disrupt the dsRNA binding. They suggest that the A–E mutation made by Poulse et al. could in fact interfere with a hydrophobic residue required for folding, and therefore could entirely disrupt the structure of the dsRBM.

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Adenosine Deaminases Acting on RNA (Adars) and A-to-I Editing by Rena A. Goodman, Mark R. Macbeth (auth.), Charles E. Samuel (eds.)


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