title: The Myxococcus xanthus pilQ (sglA) gene encodes a secretin homolog required for type IV pilus biogenesis, social motility, and development.
abstract: The Myxococcus xanthus sglA1 spontaneous mutation was originally isolated because it allowed dispersed cell growth in liquid yet retained the ability to form fruiting bodies. Consequently, most of today's laboratory strains either contain the sglA1 mutation or were derived from strains that carry it. Subsequent work showed that sglA was a gene for social gliding motility, a process which is mediated by type IV pili. Here sglA is shown to map to the major pil cluster and to encode a 901-amino-acid open reading frame (ORF) that is homologous to the secretin superfamily of proteins. Secretins form a channel in the outer membrane for the transport of macromolecules. The closest homologs found were PilQ proteins from Pseudomonas aeruginosa and Neisseria gonorrhoeae, which are required for type IV pili biogenesis and twitching motility. To signify these molecular and functional similarities, we have changed the name of sglA to pilQ. The hypomorphic pilQ1 (sglA1) allele was sequenced and found to contain two missense mutations at residues 741 (G-->S) and 762 (N-->G). In addition, 19 independent social (S)-motility mutations are shown to map to the pilQ locus. In-frame deletions of pilQ and its downstream gene, orfL, were constructed. pilQ is shown to be essential for pilus biogenesis, S-motility, rippling, and fruiting body formation, while orfL is dispensable for these processes. The pilQ1 allele, but not the DeltapilQ allele, was found to render cells hypersensitive to vancomycin, suggesting that PilQ1 alters the permeability properties of the outer membrane. Many differences between pilQ1 and pilQ+ strains have been noted in the literature. We discuss some of these observations and how they may be rationalized in the context of our molecular and functional findings.
authors.affiliation: Departments of Biochemistry and Developmental Biology, Stanford University, Stanford, California 94305, USA.dwall@cmgm.stanford.edu
authors.forename: D
authors.initials: D
authors.lastname: Wall
authors.forename: P E
authors.initials: PE
authors.lastname: Kolenbrander
authors.forename: D
authors.initials: D
authors.lastname: Kaiser
mesh_terms: D000595:Amino Acid Sequence; D001425:Bacterial Outer Membrane Proteins / Q000235:genetics* / Q000502:physiology*; D001483:Base Sequence; D002874:Chromosome Mapping; D003001:Cloning, Molecular; D017931:DNA Primers / Q000235:genetics; D004269:DNA, Bacterial / Q000235:genetics; D036781:Fimbriae Proteins; D010861:Fimbriae, Bacterial / Q000235:genetics* / Q000502:physiology*; D015964:Gene Expression Regulation, Bacterial; D018507:Gene Expression Regulation, Developmental; D005798:Genes, Bacterial; D008969:Molecular Sequence Data; D009068:Movement; D009154:Mutation; D016941:Myxococcus xanthus / Q000235:genetics* / Q000254:growth & development / Q000502:physiology*; D016366:Open Reading Frames; D015398:Signal Transduction; D013171:Spores, Bacterial / Q000235:genetics / Q000502:physiology
chemical_list: D001425:Bacterial Outer Membrane Proteins; D017931:DNA Primers; D004269:DNA, Bacterial; C084295:pilQ protein, bacteria; D036781:Fimbriae Proteins