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In M. magneticum AMB-1 (AMB-1), the mamK deletion mutant lacks the long and highly organized magnetosome chains observed in the wild-type strain (Komeili et al., 2006).
The mqoB− mutant lacks the most potent enzyme for the conversion of malate to oxaloacetate.
This mutant lacks the binding site for the catalytic p110 subunit and therefore cannot recruit p110 upon activation [17].
This mutant lacks the ability to bind to Ras effectors and therefore acts as a dominant negative mutant.
The growth phenotype of the tpx mutant in iNOS KO macrophage further demonstrated that the tpx mutant lacks the ability to decompose peroxides and nitric oxides.
The ΔDQ mutant lacks the CMA targeting motif, and was previously shown to lack CMA dependent uptake into lysosomes [21]; therefore, the double mutant ΔDQ/A53T should not be targeted to the CMA pathway and, despite the presence of the A53T mutation, should not inhibit it.
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Due to unspecific contacts, some CadC clusters were even detected in a mutant lacking the CadC-binding site20.
A K. pneumonia mutant lacking the pathogenic factor was used as the host strain.
It was possible that this mutant lacked the ability to fold the protein properly.
In addition, in a mutant lacking the CadC-binding site, most cells (81%) did not form a CadC cluster, even under CadC-activating conditions (Fig. 6b).
Consistent with this, an UNC-45 mutant lacking the UCS loop (UNC-45ΔUCSloop) is less efficiently cleaved by the protease (Supplementary Fig. 5a).
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