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Dryad

Tandem-affinity purification of OOPS-1 and SPE-11 and identification of phosphorylation sites on OOPS-1 and SPE-11

Abstract

Fertilization triggers the completion of female meiosis and launches the oocyte-to-embryo transition. C. elegans spe-11 is one of the few known paternal-effect embryonic lethal genes. We report that the sperm protein, SPE-11, forms a complex with an oocyte protein, OOPS-1 (Oocyte Partner of SPE-11) at fertilization, and that the protein complex is required for the completion of meiosis, the block to polyspermy, and eggshell formation. Tandem-affinity purification and mass spectrometry from C. elegans extracts was used to establish that OOPS-1 and SPE-11 associate. This supplemental dataset provides the mass spectrometry data supporting the finding that OOPS-1 and SPE-11 associate in C. elegans extracts. These data were analyzed and are summarized in Table 3, Table S1, and Table S2 of the manuscript. This supplemental dataset also provides evidence that both OOPS-1 and SPE-11 are phosphoproteins. The mass spectra from the tandem-affinity purifications were analyzed for instances of protein phosphorylation. This supplemental data associated with this dataset displays the mass spectra used to identify sites of phosphorylation on OOPS-1 and SPE-11. We found multiple examples in which phosphorylation was supported at high-confidence levels by multiple diagnostic b- and y-type fragment ions in the mass spectra. These phosphorylation sites are summarized in Figure 7 of the manuscript.