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This correlates well with the fact that the dually phosphorylated PPPSPXS motif upon transferred to a heterologous receptor is sufficient to activate β-catenin signaling in vivo, whereas the PPPAPXA mutant is completely inactive [34], [35], [37].
Interestingly, when the two mutations K98A and R185A are combined, the resulting APE1 double mutant is completely devoid of its DHU-, αdA-NIR and 3'→5' exonuclease activities, indicating that these two residues are indispensable for the NIR and exonuclease functions.
Therefore, the mutant is completely sterile.
In vitro, we have shown that indeed the P56S MSP mutant is completely insoluble in buffers.
Obviously, the reduction of plant height for the mutant is completely attributed to the shorter culm length.
The Δ21 24 deletion mutant is completely unable to bind to pRb and does not induce tetrasomy.
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As shown in Fig. 5A, the K189A rNSs mutant was completely inactive whereas the D159A mutant was partially active.
Indeed, the GTPase activity of N169Q mutant was completely abolished and could not be measured (Table 2).
As in the cAMP assay, the MT1-I49N mutant was completely inactive in the ERK1/2 assay (Figure 3C).
When ΔprtV, Δlap, and ΔlapX mutants were tested in the C. elegans assay, the ΔprtV mutant was completely attenuated compared to the wild-type strain.
Furthermore, in Anabaena, a patB deletion mutant was completely defective for diazotrophic growth, but in the wildtype, its expression was restricted to heterocysts [41].
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Justyna Jupowicz-Kozak
CEO of Professional Science Editing for Scientists @ prosciediting.com