Adenosine Deaminases Acting on RNA (ADARs) and A-to-I Editing [electronic resource] /
Samuel, Charles E.editor.
The objective of this CTMI volume is to provide readers with a foundation for understanding what ADARs are and how they act to affect gene expression and function. Because A-to-I editing may affect base-pairing and RNA structure, processes including translation, splicing, RNA replication, and miR and siRNA silencing may be affected.  It also is becoming increasingly apparent that ADARs may possess roles not only as enzymes that deaminate adenosine to produce inosine in RNA substrates with double-stranded character, but also as proteins independent of their catalytic property. Future studies of ADARs no doubt will provide us with additional surprises and new insights into the modulation of biological processes by the ADAR family of proteins.
Description based upon print version of record.
Adenosine Deaminases Acting on RNA (ADARs) and A-to-I Editing; Preface; Contents; Contributors; 144 ADAR Proteins: Structure and Catalytic Mechanism; Abstract; 1...The Reaction Catalyzed by ADARs; 2...The ADAR Protein Structure is Modular; 3...Overview of Structure of ADAR2 Deaminase Domain; 4...H394, C451, C516: Zn2+ Binding; 4.1 E396; 4.2 T375; 4.3 R455; 5...Residues Involved in IP6 Binding; 6...Roles of Functional Groups in RNA Substrate at or Near the Deamination Site; 7...The Effect of Helix Defects; 8...Preferred Flanking Sequence; 9...A--C Mismatch at Editing Site
10...2vprime-Hydroxyl of the Edited Nucleoside11...8-Aza Substitution at Edited Adenosine; 12...N7 of Substrate, C7 Substituents on Adenosine Analogs; 13...C6- and C2-Positions of the Edited Purine; 13.1 The ADAR Reaction Mechanism; 13.2 Dimerization; 13.3 Substrate Binding and Conformational Changes; 13.4 Deamination in the ADAR Active Site and Product Release; Acknowledgments; References; 145 ADAR Proteins: Double-stranded RNA and Z-DNA Binding Domains; Abstract; 1...Introduction; 2...Adenosine Deaminases Acting on RNA Family Members and Their Domain Organization; 3...RNA Editing Substrate
3.1 Specificity of Editing3.2 What Makes a Good Editing Site?; 3.2.1 Preferences; 3.2.2 Selectivity; 3.3 Structures of Editing Substrates; 4...Adenosine Deaminases Acting on RNA Z-DNA Binding Domains; 4.1 Z-DNA Binding Domain: Structure and Substrate Recognition; 4.2 A Role for ADAR1 Z alpha Domain?; 4.3 How Does a Z-DNA Binding Domain Bind to Z-DNA?; 4.4 ADAR1 Z beta Domain: a Domain for Protein--Protein Interaction?; 5...Adenosine Deaminases Acting on RNA dsRNA Binding Domains; 5.1 Structural Characteristics of a dsRNA Binding Domain; 5.2 Sequence Specific Recognition with dsRBD
5.3 How dsRBDs are Positioned on Substrate?5.4 Are the Binding Sites of ADAR dsRBDs Predictable?; 6...dsRBDs and Z-DNA Binding Domains Act on the Subcellular Localization of ADARs; 7...Concluding Remarks; Acknowledgments; References; 157 Editing of Neurotransmitter Receptor and Ion Channel RNAs in the Nervous System; Abstract; 1...Introduction; 2...Identification of A-to-I Editing Targets; 3...Mammalian ADAR Enzymes; 4...ADAR Substrates in the Central Nervous System; 4.1 Glutamate-Gated Ion Channels; 4.1.1 AMPA Receptors; 4.1.2 Kainate Receptors; 4.2 The Serotonin 2C Receptor (5HT2C)
4.3 The alpha 3 Subunit of the GABAA Receptor (Gabra3)4.4 Voltage-gated Potassium Channel (Kv1.1); 5...Conclusions; References; 151 Modulation of MicroRNA Expression and Function by ADARs; Abstract; 1...Introduction; 2...MiRNA Biogenesis and Function; 3...Editing of MiRNAs; 3.1 Identification of Pri-MiRNA Editing Sites; 3.1.1 Systematic Surveys for MiRNA Editing Sites; 3.1.2 High-Throughput Sequencing of Mature MiRNAs; 3.2 Consequences of Pri-MiRNA Editing; 3.2.1 Effect on Drosha Cleavage; 3.2.2 Degradation of Inosine-Containing Pri-MiRNAs; 3.2.3 Effect on Dicer Cleavage; 3.2.4 Effect on RISC Loading
3.2.5 Effect on Mature MiRNA Function
Includes bibliographical references and index.
The objective of this CTMI volume is to provide readers with a foundation for understanding what ADARs are and how they act to affect gene expression and function. Because A-to-I editing may affect base-pairing and RNA structure, processes including translation, splicing, RNA replication, and miR and siRNA silencing may be affected.  It also is becoming increasingly apparent that ADARs may possess roles not only as enzymes that deaminate adenosine to produce inosine in RNA substrates with double-stranded character, but also as proteins independent of their catalytic property. Future studies of ADARs no doubt will provide us with additional surprises and new insights into the modulation of biological processes by the ADAR family of proteins.
Molecular biology.
Human physiology.
Molecular Medicine.
Human Physiology.


Current Topics in Microbiology and Immunology