The Enzymatic Activity of APOBE3G Multimers.

Abstract:

:APOBEC3G (A3G) belongs to the family of cytosine deaminases that play an important role in the innate immune response. Similar to other, two-domain members of the APOBEC family, A3G is prone to concentration-dependent oligomerization, which is an integral for its function in the cell. It is shown that oligomerization of A3G is related to the packing mechanism into virus particle and, is critical for the so-called roadblock model during reverse transcription of proviral ssDNA. The role of oligomerization for deaminase activity of A3G is widely discussed in the literature; however, its relevance to deaminase activity for different oligomeric forms of A3G remains unclear. Here, using Atomic Force Microscopy, we directly visualized A3G-ssDNA complexes, determined their yield and stoichiometry and in parallel, using PCR assay, measured the deaminase activity of these complexes. Our data demonstrate a direct correlation between the total yield of A3G-ssDNA complexes and their total deaminase activity. Using these data, we calculated the relative deaminase activity for each individual oligomeric state of A3G in the complex. Our results show not only similar deaminase activity for monomer, dimer and tetramer of A3G in the complex, but indicate that larger oligomers of A3G retain their deaminase activity.

journal_name

Sci Rep

journal_title

Scientific reports

authors

Pan Y,Zagorski K,Shlyakhtenko LS,Lyubchenko YL

doi

10.1038/s41598-018-36372-6

subject

Has Abstract

pub_date

2018-12-18 00:00:00

pages

17953

issue

1

issn

2045-2322

pii

10.1038/s41598-018-36372-6

journal_volume

8

pub_type

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