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

“The target of this CTMI quantity is to supply readers with a origin for knowing what ADARs are and the way they act to impact gene expression and serve as. it really 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 autonomous in their catalytic estate. simply because A-to-I enhancing may perhaps impact base-pairing and RNA constitution, approaches together with translation, splicing, RNA replication, and miR and siRNA silencing can be affected. destiny stories of ADARs doubtless will offer us with extra surprises and new insights into the modulation of organic approaches via the ADAR relations of proteins.”

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ADAR1 has two related Z-DNA binding domains named Za and Zb (Fig. 2), the latter one having no binding capacity for Z-DNA. In this section we review the structural knowledge on ADAR1 Z-DNA binding domains and especially on the binding of Za to Z-DNA. 1 Z-DNA Binding Domain: Structure and Substrate Recognition The first structural information about Z-DNA binding domains and the molecular basis of the recognition of Z-DNA was revealed together by the crystal structure of the human Za domain of ADAR1 complexed to DNA (Schwartz et al.

We also review the current structural knowledge of another type of nucleic acid binding domain present in ADARs, namely the Z-DNA binding domains. 2 Adenosine Deaminases Acting on RNA Family Members and Their Domain Organization Adenosine deaminases acting on RNA proteins were first discovered in Xenopus laevis (Rebagliati and Melton 1987; Bass and Weintraub 1987, 1988) and have now been characterized in nearly all metazoa from worm to man (Tonkin et al. 2002; Palladino et al. 2000; Slavov et al.

1997). This renders it unique among the members of ADAR protein family (Fig. 2a). Actually, ADAR1 is expressed in two isoforms: the interferon-inducible ADAR1-i (inducible; 150 kDa) and the constitutively expressed ADAR1-c (constitutive; 110 kDa) which is initiated from a downstream methionine as the result of alternativesplicing and skipping of the exon containing the upstream methionine (Patterson and Samuel 1995; Patterson et al. 1995; Kawakubo and Samuel 2000). As a consequence, the short version of ADAR1 lacks the N-terminal Z-DNA binding domain (Fig.

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