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ADAR Proteins: Structure and Catalytic Mechanism

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Book cover Adenosine Deaminases Acting on RNA (ADARs) and A-to-I Editing

Part of the book series: Current Topics in Microbiology and Immunology ((CT MICROBIOLOGY,volume 353))

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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Acknowledgments

P.A.B would like to acknowledge support from the National Institutes of Health in the form of grant R01GM061115. R.A.G is supported by a Graduate Research Fellowship from the National Science Foundation.

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Authors and Affiliations

  1. Department of Chemistry, University of California, One Shields Ave, Davis, CA, 95616, USA

    Rena A. Goodman & Peter A. Beal

  2. Department of Biological Sciences, Carnegie Mellon University, 4400 Fifth Avenue, Pittsburgh, PA, 15213, USA

    Mark R. Macbeth

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  1. Rena A. Goodman
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  2. Mark R. Macbeth
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Correspondence to Mark R. Macbeth or Peter A. Beal .

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  1. , Dept. of Molecular, Cellular and Develop, University of California, Santa Barbara, Santa Barbara, 93106, California, USA

    Charles E. Samuel

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Goodman, R.A., Macbeth, M.R., Beal, P.A. (2011). ADAR Proteins: Structure and Catalytic Mechanism. In: Samuel, C. (eds) Adenosine Deaminases Acting on RNA (ADARs) and A-to-I Editing. Current Topics in Microbiology and Immunology, vol 353. Springer, Berlin, Heidelberg. https://doi.org/10.1007/82_2011_144

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