Category:MichSt14A 47

Figure S4A shows that OGFOD1 does in vitro hydroxylation of a peptide derived from RPS23, assayed by mass spec.

Figure 5 shows that OGFOD1 knockouts are less likely to terminate at a nonsense codon. This implies that OGFOD1 modulates translation termination efficiency. A catalytically inactive mutant also terminates earlier, similar to the knockout. This suggests that it is the ribosomal binding function of OGFOD1 that regulates the translational termination.

See Figure 3. In A, a 100-kDa species in an immunoprecipitation is consistent with the weight of a hypothetical OGFOD1-RPS23 complex. Other experiments on this figure support this. RPS23 is a ribosomal binding site.

See Figure 1

See Figure 4.

See Table 1 and Figure 2.

See Table 1 and Figure 2.

Figure 1 shows that the SCF complex (Cul1 and Skp1) is required for Ku80 ubiquitylation. Ku80 is the initiating factor of nonhomologous end joining double-strand break repair. When polyubiquitylated, Ku80 dissociates from the DNA where the break was. Figure 4 (an immunoprecipitation) shows that when Fbxl2 is not present, the binding of Cul1 and Skp1 is inhibited and there are less modifications to Ku80. This proves that Fbx12 is the protein that recruits the SCF to double stranded breaks.