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Published 26 April 2004. doi:10.1083/jcb.200311040
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 165, Number 2, 233-242
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Article

Fascin-mediated propulsion of Listeria monocytogenes independent of frequent nucleation by the Arp2/3 complex



William M. Brieher, Margaret Coughlin, and Timothy J. Mitchison

Department of Systems Biology, Harvard University Medical School, Boston, MA 02115

Address correspondence to William M. Brieher, Dept. of Systems Biology, Harvard University Medical School, 250 Longwood Ave., SGM-523, Boston, MA 02115. Tel.: (617) 432-3724. Fax: (617) 432-3702. email: bill_brieher{at}hms.harvard.edu

Actin-dependent propulsion of Listeria monocytogenes is thought to require frequent nucleation of actin polymerization by the Arp2/3 complex. We demonstrate that L. monocytogenes motility can be separated into an Arp2/3-dependent nucleation phase and an Arp2/3-independent elongation phase. Elongation-based propulsion requires a unique set of biochemical factors in addition to those required for Arp2/3-dependent motility. We isolated fascin from brain extracts as the only soluble factor required in addition to actin during the elongation phase for this type of movement. The nucleation reaction assembles a comet tail of branched actin filaments directly behind the bacterium. The elongation-based reaction generates a hollow cylinder of parallel bundles that attach along the sides of the bacterium. Bacteria move faster in the elongation reaction than in the presence of Arp2/3, and the rate is limited by the concentration of G-actin. The biochemical and structural differences between the two motility reactions imply that each operates through distinct biochemical and biophysical mechanisms.

Key Words: actin; Arp2/3; fascin; filopodia; Listeria

Abbreviations used in this paper: AMPPNP, adenosine 5'-(ß,{gamma}-imido)triphosphate; ß-Me, ß-mercaptoethanol; CA; cofilin homology and acidic region of N-WASP; Ptk, rat kangaroo kidney; TMR, tetramethylrhodamine.


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