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

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.