Interactions of APOBEC3s with DNA and RNA

•Specificity of APOBEC3 proteins is determined by 4 active site loops•ssDNA adopts different conformations dependent on the APOBEC3 enzyme•Regions remote from the active site, including the N-terminal domain, contribute to substrate DNA and RNA binding sites. APOBEC3 enzymes are key enzymes in our i...

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Published inCurrent opinion in structural biology Vol. 67; pp. 195 - 204
Main Authors Maiti, Atanu, Hou, Shurong, Schiffer, Celia A, Matsuo, Hiroshi
Format Journal Article
LanguageEnglish
Published England Elsevier Ltd 01.04.2021
Subjects
APOBEC Deaminases - metabolism
DNA
RNA
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Summary:•Specificity of APOBEC3 proteins is determined by 4 active site loops•ssDNA adopts different conformations dependent on the APOBEC3 enzyme•Regions remote from the active site, including the N-terminal domain, contribute to substrate DNA and RNA binding sites. APOBEC3 enzymes are key enzymes in our innate immune system regulating antiviral response in HIV and unfortunately adding diversity in cancer as they deaminate cytosine. Seven unique single and double domain APOBEC3s provide them with unique activity and specificity profiles for this deamination. Recent crystal and NMR structures of APOBEC3 complexes are unraveling the variety of epitopes involved in binding nucleic acids, including at the catalytic site, elsewhere on the catalytic domain and in the inactive N-terminal domain. The interplay between these diverse interactions is critical to uncovering the mechanisms by which APOBEC3s recognize and process their substrates.
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Joint first authors: atanu.maiti@nih.gov, Shurong.Hou@umassmed.edu
The International Committee of Medical Journal Editors (ICMJE) recommends that authorship be based on the following four criteria
3. Final approval of the version to be published; AND
Authorship
1. Substantial contributions to the conception or design of the work; or the acquisition, analysis, or interpretation of data for the work; AND
2. Drafting the work or revising it critically for important intellectual content; AND
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ISSN:0959-440X
1879-033X
DOI:10.1016/j.sbi.2020.12.004