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Abstract

We describe the characterization in Xenopus laevis of a nuclear protein, xnf7, which is first detected in the oocyte GV and is eventually enriched in nuclei of cells of the adult brain. Previous studies have shown that this protein contains zinc-finger-like structures and acidic domains typical of transcriptional activators, and is phosphorylated in vitro by p34cdc2 protein kinase. The protein also binds to double-stranded DNA. These data suggest that xnf7 may function as a transcription factor. During oocyte maturation, xnf7 is released into the cytoplasm and is not detectable in nuclei until the mid-blastula-gastrula stage of development. Western blot analysis of xnf7 isolated from oocytes and eggs showed the existence of multiple bands or isoforms of the protein. Unique isoforms that are generated during oocyte maturation are the result of phosphorylation. The phosphorylated isoforms remain in the cytoplasm until the mid-blastula stage. The re-accumulation of protein in the embryonic nuclei at this time correlates with the increase in abundance of the less phosphorylated isoforms. The xnf7 protein possesses a nuclear localization signal (NLS) similar to the bipartite signal found in nucleoplasmin. Newly synthesized xnf7 accumulated in the oocyte GV to detectable levels within a few hours following synthesis suggesting that retention of the protein in the cytoplasm during early cleavage may be due to a process that interferes with the function of the NLS. These data suggest that compartmentalization and/or post-translational modification of the nuclear protein xnf7 may be involved in regulating its function during early development.