Antiviral protein APOBEC3G localizes to ribonucleoprotein complexes found in P bodies and stress granules.

ABSTRACT: Members of the APOBEC (apolipoprotein B mRNA-editing enzyme catalytic polypeptide 1-like) family of cytidine deaminases inhibit host cell genome invasion by exogenous retroviruses and endogenous retrotransposons. Because these enzymes can edit DNA or RNA and potentially mutate cellular targets, their activities are presumably regulated; for instance, APOBEC3G (A3G) recruitment into high-molecular-weight ribonucleoprotein (RNP) complexes has been shown to suppress its enzymatic activity. We used tandem affinity purification together with mass spectrometry (MS) to identify protein components within A3G-containing RNPs. We report that numerous cellular RNA-binding proteins with diverse roles in RNA function, metabolism, and fate determination are present in A3G RNPs but that most interactions

SUBMITTER: Gallois-Montbrun S 

PROVIDER: S-EPMC1865933 | biostudies-literature | 2007 Mar

REPOSITORIES: biostudies-literature