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Interaction of APOBEC3A with DNA assessed by atomic force microscopy
Luda S Shlyakhtenko1, Alexander J Lushnikov1, Ming Li2
1Department of Pharmaceutical Sciences, College of Pharmacy, University of Nebraska Medical Center, Omaha, Nebraska, United States of America.
Plos One
|June 7, 2014
Summary
APOBEC3A (A3A) DNA deaminase binds single-stranded DNA, primarily as a monomer. This contrasts with APOBEC3G, highlighting unique biophysical properties of A3A relevant to innate immunity.
Area of Science:
- Biochemistry
- Molecular Biology
- Immunology
Background:
- The APOBEC3 family of DNA cytosine deaminases inhibits retroelements and retroviruses like HIV-1.
- APOBEC3A (A3A) is unique, expressed in myeloid cells, induced by interferon, and acts on various DNA bases.
Purpose of the Study:
- To characterize the interaction between APOBEC3A and DNA using atomic force microscopy (AFM).
- To investigate the oligomeric state of APOBEC3A when bound to DNA and in solution.
Main Methods:
- Atomic Force Microscopy (AFM) was used to analyze APOBEC3A binding to hybrid DNA (single-stranded region flanked by duplexes).
- AFM image analysis quantified complex formation and determined the oligomeric state of APOBEC3A.
Main Results:
- APOBEC3A binds to single-stranded DNA, with high complex yield (∼80%) at high protein-to-DNA ratios (≥100:1).
- APOBEC3A is predominantly monomeric when bound to single-stranded DNA and in solution up to 50 nM.
- These findings contrast with APOBEC3G, which tends to oligomerize.
Conclusions:
- APOBEC3A exhibits distinct biophysical properties compared to APOBEC3G.
- These differences may relate to APOBEC3A's role in innate immunity.
