• BMB Reports
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• 제42권1호
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• pp.22-27
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• 2009

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 $\alpha$ ($RIP{\alpha}$) was originally identified as a nuclear transporter of RPA in Xenopus. The human $RIP{\alpha}$ gene encodes several splice isoforms, of which $hRIP{\alpha}$ and $hRIP{\beta}$ are the major translation products in vivo. However, limited information is available about the alternative splicing of $RIP{\alpha}$ in eukaryotes, apart from that in humans. In this study, we examined the alternative splicing of RIP{\alpha} in the Drosophila, Xenopus, and mouse system. We showed that the number of splice isoforms of RIP{\alpha} was species-specific, and displayed a tendency to increase in higher eukaryotes. Moreover, a mouse ortholog of $hRIP{\alpha}$, $mRIP{\beta}2$, was not SUMOylated, in contrast to $hRIP{\alpha}$. Based on these results, we suggest that the $RIP{\alpha}$ gene gains more splice isoforms and additional modifications after molecular evolution.