title: Social motility in Myxococcus xanthus requires FrzS, a protein with an extensive coiled-coil domain.
abstract: Gliding motility in the developmental bacterium Myxococcus xanthus involves two genetically distinct motility systems, designated adventurous (A) and social (S). Directed motility responses, which facilitate both vegetative swarming and developmental aggregation, additionally require the 'frizzy' (Frz) signal transduction pathway. In this study, we have analysed a new gene (frzS), which is positioned upstream of the frzA-F operon. Insertion mutations in frzS caused both vegetative spreading and developmental defects, including 'frizzy' aggregates in the FB strain background. The 'frizzy' phenotype was previously considered to result only from defective directed motility responses. However, deletion of the frzS gene in an A-S+ motility background demonstrated that FrzS is a new component of the S-motility system, as the A-frzS double mutant was non-spreading (A-S-). Compared with known S-motility mutants, the frzS mutants appear similar to pilT mutants, in that both produce type IV pili, extracellular fibrils and lipopolysaccharide (LPS) O-antigen, and both agglutinate rapidly in a cohesion assay. The FrzS protein has an unusual domain composition for a bacterial protein. The N-terminal domain shows similarity to the receiver domains of the two-component response regulator proteins. The C-terminal domain is composed of up to 38 heptad repeats (a b c d e f g)38, in which residues at positions a and d are predominantly hydrophobic, whereas residues at positions e and g are predominantly charged. This periodic disposition of specific residues suggests that the domain forms a long coiled-coil structure, similar to those found in the alpha-fibrous proteins, such as myosin. Overexpression of this domain in Escherichia coli resulted in the formation of an unusual striated protein lattice that filled the cells. We speculate on the role that this novel protein could play in gliding motility.
authors.affiliation: Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720-3204, USA.
authors.forename: M J
authors.initials: MJ
authors.lastname: Ward
authors.forename: H
authors.initials: H
authors.lastname: Lew
authors.forename: D R
authors.initials: DR
authors.lastname: Zusman
mesh_terms: D001426:Bacterial Proteins / Q000235:genetics* / Q000378:metabolism; D003001:Cloning, Molecular; D019281:Dimerization; D004926:Escherichia coli / Q000235:genetics; D010861:Fimbriae, Bacterial / Q000235:genetics; D017353:Gene Deletion; D008969:Molecular Sequence Data; D009154:Mutation; D016941:Myxococcus xanthus / Q000166:cytology* / Q000235:genetics*; D011487:Protein Conformation; D017421:Sequence Analysis
chemical_list: D001426:Bacterial Proteins; C415990:FrzS protein, Myxococcus xanthus