Atomic force microscopy studies of APOBEC3G oligomerization and dynamics.

ABSTRACT: The DNA cytosine deaminase APOBEC3G (A3G) is a two-domain protein that binds single-stranded DNA (ssDNA) largely through its N-terminal domain and catalyzes deamination using its C-terminal domain. A3G is considered an innate immune effector protein, with a natural capacity to block the replication of retroviruses such as HIV and retrotransposons. However, knowledge about its biophysical properties and mechanism of interaction with DNA are still limited. Oligomerization is one of these unclear issues. What is the stoichiometry of the free protein? What are the factors defining the oligomeric state of the protein? How does the protein oligomerization change upon DNA binding? How stable are protein oligomers? We address these questions here using atomic force microscopy (AFM) to directly ima

SUBMITTER: Shlyakhtenko LS 

PROVIDER: S-EPMC3844295 | biostudies-literature | 2013 Nov

REPOSITORIES: biostudies-literature