Extended Data Table 2 ADP-ribosylation of rS1-WT, -R139K and -R139A during T4 phage infection

From: A viral ADP-ribosyltransferase attaches RNA chains to host proteins

  1. MaxQuant intensities are presented for T4 phage-infected and uninfected samples in biologically independent triplicates (n = 3) only for the respective peptide of the R139 mutation site which is expected for the respective rS1 version. ADP-ribosylation of the peptide in rS1 is observed in vivo in all three replicates. However, ADP-ribosylation at position 139 is abolished by R139A or R139K mutations (mutation indicated in red). The intensity of ADP-ribosylated peptide relative to the intensity of the corresponding unmodified peptide species is at least 3-fold reduced upon R139 mutation. One may speculate that R142 is nevertheless ADP-ribosylated in the mutated rS1 proteins but overall ADP-ribosylation yield at the peptide may be reduced as the potentially predominant ADP-ribosylation site (R139) is not available for modification.
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