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International audience; The murine PL10 cDNA corresponds to a transcript expressed only in the male germ line. Its expression is developmentally regulated, with high levels of transcripts being present during the meiotic and haploid stages of spermatogenesis. The deduced protein is shown to be highly homologous to the murine translation initiation factor eIF-4A and to other proteins that are also homologous to eIF-4A, including the Drosophila protein vasa. By consensus sequence conservation and comparison of secondary structure predictions, putative mononucleotide binding and DNA/RNA binding domains are proposed to be shared by all these proteins. Taken together, these results suggest a helicase function for PL10 protein similar to that of eIF-4A and suggests its possible role in a key step of the spermatogenic process. The possible significance of the similarity between the PL10 protein and the protein product of the maternal effect gene vasa is also discussed.

International audience; The immunopurified yeast DNA polymerase--DNA primase complex is constituted by DNA polymerase I polypeptides and by three other protein species, called p74, p58 and p48, which we show to be immunologically unrelated. The gene encoding the p48 polypeptide has been identified by immunological screening of a lambda gt11 yeast genomic DNA library. Antiserum specific for p48 inhibits DNA primase, and immunoreactive, inhibitory antibodies are affinity-purified by the clone-encoded protein, thus relating the p48 polypeptide to DNA primase activity. The entire gene has been cloned, and the 1.45-kb p48 mRNA is overproduced in cells containing the gene in high copy number. Gene disruption and Southern hybridization experiments demonstrate that the p48 protein is encoded by a single gene and it performs an essential function.