Replication Protein A (RPA) is a single stranded DNA-binding protein involved in DNA metabolic activities such as replication, repair, and recombination. RPA-Interacting Protein α (RIPα) was originally identified as a nuclear transporter of RPA in Xenopus. The human RIPα gene encodes several splice isoforms, of which hRIPα and hRIPβ are the major translation products in vivo. However, limited information is available about the alternative splicing of RIPα in eukaryotes, apart from that in humans. In this study, we examined the alternative splicing of RIPα in the Drosophila, Xenopus, and mouse system. We showed that the number of splice isoforms of RIPα was species-specific, and displayed a tendency to increase in higher eukaryotes. Moreover, a mouse ortholog of hRIPβ, mRIPβ2, was not SUMOylated, in contrast to hRIPβ. Based on these results, we suggest that the RIPα gene gains more splice isoforms and additional modifications after molecular evolution.
All Science Journal Classification (ASJC) codes
- Molecular Biology