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Journal of Bacteriology, March 2002, p. 1678-1684, Vol. 184, No. 6
0021-9193/02/$04.00+0     DOI: 10.1128/JB.184.6.1678-1684.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

An Extracellular Matrix-Associated Zinc Metalloprotease Is Required for Dilauroyl Phosphatidylethanolamine Chemotactic Excitation in Myxococcus xanthus

Daniel B. Kearns,1,{dagger} Pamela J. Bonner,1 Daniel R. Smith,2 and Lawrence J. Shimkets1*

Department of Microbiology, University of Georgia, Athens, Georgia 30602,1 Department of Biology, Seattle University, Seattle, Washington 981222

Received 13 September 2001/ Accepted 20 December 2001

An extracellular matrix connects bacteria that live in organized assemblages called biofilms. While the role of the matrix in the regulation of cell behavior has not been extensively examined in bacteria, we suggest that, like mammalian cells, the matrix facilitates cell-cell interactions involved with regulation of cohesion, motility, and sensory transduction. The extracellular matrix of the soil bacterium Myxococcus xanthus is essential for biofilm formation and fruiting body development. The matrix material is extruded as long, thin fibrils that mediate adhesion to surfaces, cohesion to other cells, and excitation by the chemoattractant dilauroyl phosphatidylethanolamine. We report the identification of a putative matrix-associated zinc metalloprotease called FibA (fibril protein A). Western blotting with FibA-specific monoclonal antibody 2105 suggests extensive proteolytic processing of FibA during assembly into fibrils, consistent with the autoprocessing observed with other members of the M4 metalloprotease family. Disruption of fibA had no obvious effect on the structure of the fibrils and did not inhibit cell cohesion, excitation by dioleoyl phosphatidylethanolamine, or activity of the A- or S-motility motors. However, the cells lost the ability to respond to dilauroyl phosphatidylethanolamine and to form well-spaced fruiting bodies, though substantial aggregation was observed. Chemotactic excitation of the fibA mutant was restored by incubation with purified wild-type fibrils. The results suggest that this metalloprotease is involved in sensory transduction.

* Corresponding author. Mailing address: Department of Microbiology, University of Georgia, 527 Biological Sciences Building, Athens, GA 30602. Phone: (706) 542-2681. Fax: (706) 542-2674. E-mail: Shimkets{at}arches.uga.edu.

{dagger} Present address: Department of Molecular and Cellular Biology, Harvard University, Cambridge, MA 02138.

Journal of Bacteriology, March 2002, p. 1678-1684, Vol. 184, No. 6
0021-9193/02/$04.00+0     DOI: 10.1128/JB.184.6.1678-1684.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



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