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Journal of Bacteriology, January 1999, p. 24-33, Vol. 181, No. 1
Departments of Biochemistry and Developmental
Biology, Stanford University, Stanford, California
94305,1 and
Oral Infection and
Immunity Branch, National Institute of Dental and Craniofacial
Research, National Institutes of Health, Bethesda, Maryland
208922
Received 13 August 1998/Accepted 26 October 1998
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
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
The Myxococcus xanthus pilQ
(sglA) Gene Encodes a Secretin Homolog Required for Type IV
Pilus Biogenesis, Social Motility, and Development
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
pilQ 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.
*
Corresponding author. Mailing address: Departments of
Biochemistry and Developmental Biology, Stanford University, Stanford, CA 94305. Phone: (650) 723-5685. Fax: (650) 725-7739. E-mail: dwall{at}cmgm.stanford.edu.
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