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As expected, the escN null mutant, which is a T3SS ATPase mutant, exhibited very low translocation ability, due to its inability to secrete and translocate effector proteins (Fig. 6B).

Strikingly, we found that the T162A mutant exhibited very low activity and was not further activated by serum starvation, whereas the T162E mutant showed high activity but was also not further activated (Fig.  7C and D).

Interestingly, in both cases (i.e., with and without cytochrome c) we found that the Y120A/P121A HCCS mutant exhibited very little spectral evidence of heme binding, which was also consistent with the heme stain analysis of the purified protein.

Strikingly, these mutants exhibited very different phenotypes: while the S103A substitution does not change the PA66 phenotype, the S103D mutation inactivates the BicDA40V protein, causing BicDA40V, S103D to behave as a null mutant.

Three of the Ago1 missense mutants exhibited very mild mispatterning, and the fourth mutant, Ago1 R937C, had a small necrotic eye (data not shown).

In contrast to these results, PA-G342A bound ANTXR2-expressing cells at a level similar to that of wild-type PA, and the remaining mutants exhibited very low levels of binding.

Next we analyzed immunolocalization of pan-twinfilin in auditory epithelia of Whrnwi/wi and Myo15a sh2/sh2 mice as these mutants exhibit very short stereocilia and tips of all stereocilia within single bundles contain myosinVIIa [5].

The wild-type, vps27 ∆, and wsc1 ∆ mutants exhibit very few single cells in comparison (Sarode et al. 2011).

Not unexpectedly, the L22P mutant exhibits very low activity when it is assayed at substrate concentrations that would saturate the wild-type enzyme.

In the absence of CPA, the mutant exhibits very slow gating kinetics and several conductive states (Fig. 10) that were not found for F256A, but which are of the same order of magnitude of the conductance of F256A (0.4 pA–1.9 pA) (Fig. 10B, C).

Given that the single mutant mice exhibited very mild or no phenotype, we postulated that the two secreted sulfatases perform redundant function(s) in vivo.