An oocyte-preferential histone mRNA stem-loop-binding protein like is expressed in several mammalian species.

During early embryo development, chromatin packaging is sustained by histones of maternal origin. Most histone messenger RNAs are not polyadenylated, but rather end in an evolutionarily conserved stem-loop that controls RNA processing, nucleocytoplasmic transport, stability, and translation via interactions with a specific protein named stem-loop-binding protein (SLBP). In mouse oocytes, mSLBP is synthesized abundantly during maturation and activates histone translation. In Xenopus, xSLBP is present in stage-VI oocytes, but histone mRNA is protected from premature translation by the oocyte-specific Xenopus SLBP2 (xSLBP2) protein; during maturation xSLBP2 replacement by xSLBP results in histone synthesis. Here, we report the first experimental evidence and characterization of a mammalian SLBP2 ortholog. Bovine bSLBP and bSLBP2 display distinct expression patterns throughout oocyte maturation and pre-implantation embryo development. From the immature oocyte to the morula, bSLBP2 is concentrated in the nucleus, while it is homogeneously distributed throughout the cytoplasm in mature oocytes. A putative SLBP2 gene is conserved in the genome of several mammalian species, and the corresponding transcripts were detected in rat, dog, horse, and pig oocytes. By contrast, a pseudogene is found in mouse, human, and rabbit. Altogether, our data suggest that the availability of histones in oocytes is regulated by an alternative mechanism in bovine and other species as compared to mouse and frog.