AglZ is a filament-forming coiled-coil protein required for adventurous gliding motility of Myxococcus xanthus |
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Authors: | Yang Ruifeng Bartle Sarah Otto Rebecca Stassinopoulos Angela Rogers Matthew Plamann Lynda Hartzell Patricia |
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Institution: | Department of Microbiology, Molecular Biology, and Biochemistry, University of Idaho, Moscow, ID 83844, USA. |
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Abstract: | The aglZ gene of Myxococcus xanthus was identified from a yeast two-hybrid assay in which MglA was used as bait. MglA is a 22-kDa cytoplasmic GTPase required for both adventurous and social gliding motility and sporulation. Genetic studies showed that aglZ is part of the A motility system, because disruption or deletion of aglZ abolished movement of isolated cells and aglZ sglK double mutants were nonmotile. The aglZ gene encodes a 153-kDa protein that interacts with purified MglA in vitro. The N terminus of AglZ shows similarity to the receiver domain of two-component response regulator proteins, while the C terminus contains heptad repeats characteristic of coiled-coil proteins, such as myosin. Consistent with this motif, expression of AglZ in Escherichia coli resulted in production of striated lattice structures. Similar to the myosin heavy chain, the purified C-terminal coiled-coil domain of AglZ forms filament structures in vitro. |
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