AglZ Is a Filament-Forming Coiled-Coil Protein Required for Adventurous Gliding Motility ofMyxococcus xanthus
Open Access
- 15 September 2004
- journal article
- research article
- Published by American Society for Microbiology in Journal of Bacteriology
- Vol. 186 (18), 6168-6178
- https://doi.org/10.1128/jb.186.18.6168-6178.2004
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.Keywords
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