Literature DB >> 21769729

ADAR proteins: structure and catalytic mechanism.

Rena A Goodman1, Mark R Macbeth, Peter A Beal.   

Abstract

Since the discovery of the adenosine deaminase (ADA) acting on RNA (ADAR) family of proteins in 1988 (Bass and Weintraub, Cell 55:1089-1098, 1988) (Wagner et al. Proc Natl Acad Sci U S A 86:2647-2651, 1989), we have learned much about their structure and catalytic mechanism. However, much about these enzymes is still unknown, particularly regarding the selective recognition and processing of specific adenosines within substrate RNAs. While a crystal structure of the catalytic domain of human ADAR2 has been solved, we still lack structural data for an ADAR catalytic domain bound to RNA, and we lack any structural data for other ADARs. However, by analyzing the structural data that is available along with similarities to other deaminases, mutagenesis and other biochemical experiments, we have been able to advance the understanding of how these fascinating enzymes function.

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Year:  2012        PMID: 21769729     DOI: 10.1007/82_2011_144

Source DB:  PubMed          Journal:  Curr Top Microbiol Immunol        ISSN: 0070-217X            Impact factor:   4.291


  29 in total

Review 1.  A role for the base excision repair enzyme NEIL3 in replication-dependent repair of interstrand DNA cross-links derived from psoralen and abasic sites.

Authors:  Zhiyu Yang; Maryam Imani Nejad; Jacqueline Gamboa Varela; Nathan E Price; Yinsheng Wang; Kent S Gates
Journal:  DNA Repair (Amst)       Date:  2017-02-20

2.  RNA-Seq analysis identifies a novel set of editing substrates for human ADAR2 present in Saccharomyces cerevisiae.

Authors:  Tristan Eifler; Subhash Pokharel; Peter A Beal
Journal:  Biochemistry       Date:  2013-10-31       Impact factor: 3.162

Review 3.  ADARs: viruses and innate immunity.

Authors:  Charles E Samuel
Journal:  Curr Top Microbiol Immunol       Date:  2012       Impact factor: 4.291

4.  A conserved glutamate residue in the C-terminal deaminase domain of pentatricopeptide repeat proteins is required for RNA editing activity.

Authors:  Michael L Hayes; Kim N Dang; Michael F Diaz; R Michael Mulligan
Journal:  J Biol Chem       Date:  2015-03-04       Impact factor: 5.157

5.  Specificity of the double-stranded RNA-binding domain from the RNA-activated protein kinase PKR for double-stranded RNA: insights from thermodynamics and small-angle X-ray scattering.

Authors:  Sunita Patel; Joshua M Blose; Joshua E Sokoloski; Lois Pollack; Philip C Bevilacqua
Journal:  Biochemistry       Date:  2012-11-09       Impact factor: 3.162

6.  The dsRBP and inactive editor ADR-1 utilizes dsRNA binding to regulate A-to-I RNA editing across the C. elegans transcriptome.

Authors:  Michael C Washburn; Boyko Kakaradov; Balaji Sundararaman; Emily Wheeler; Shawn Hoon; Gene W Yeo; Heather A Hundley
Journal:  Cell Rep       Date:  2014-02-06       Impact factor: 9.423

Review 7.  Emergency Services of Viral RNAs: Repair and Remodeling.

Authors:  Vadim I Agol; Anatoly P Gmyl
Journal:  Microbiol Mol Biol Rev       Date:  2018-03-14       Impact factor: 11.056

Review 8.  Post-transcriptional regulation of LINE-1 retrotransposition by AID/APOBEC and ADAR deaminases.

Authors:  Elisa Orecchini; Loredana Frassinelli; Silvia Galardi; Silvia Anna Ciafrè; Alessandro Michienzi
Journal:  Chromosome Res       Date:  2018-02-02       Impact factor: 5.239

9.  1.92 Angstrom Zinc-Free APOBEC3F Catalytic Domain Crystal Structure.

Authors:  Nadine M Shaban; Ke Shi; Ming Li; Hideki Aihara; Reuben S Harris
Journal:  J Mol Biol       Date:  2016-04-30       Impact factor: 5.469

10.  Catalytic zinc site and mechanism of the metalloenzyme PR-AMP cyclohydrolase.

Authors:  Robert L D'Ordine; Rebecca S Linger; Carolyn J Thai; V Jo Davisson
Journal:  Biochemistry       Date:  2012-07-09       Impact factor: 3.162

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