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  • 1
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 28 (1994), S. 346-358 
    ISSN: 0886-1544
    Keywords: Listeria monocytogenes ; actin ; alpha-actinin ; actin polymerization ; assembly ; disassembly ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Listeria monocytogenes can penetrate and multiply within a variety of cell types, including the PtK2 kidney epithelial line. Once released within the cytoplasm, L. monocytogenes acquires the capacity for rapid movement through the host cell [Dabiri et al., 1990: Proc. Natl. Acad. Sci. 87:6068-6072]. In the process, actin monomers are inserted in proximity to one end of the bacterium, forming a column or tail of actin filaments [Sanger et al., 1992: Infect. Immun. 60:3609-3619]. The rate of new actin filament growth correlates closely with the speed of bacterial migration. In this study we have used fluorescently labeled actin and alpha-actinin to monitor the movement and turnover rate of actin and alpha-actinin molecules in the tails. The half-lives of the actin and alpha-actinin present in the tails are approximately the same: actin, 58.7 sec; alpha-actinin, 55.3 sec. The half-life of alpha-actinin surrounding a dividing bacterium was 30 sec, whereas its half-life in the tails that formed behind the two daughter cells was about 20-30% longer. We discovered that the speeds of the bacteria are not constant, but show aperiodic episodes of decreased and increased speeds. There is a fluctuation also in the intensities of the fluorescent probes at the bacterium/tail interface, implying that there is a fluctuation in the number of actin filaments forming there. There was no strong correlation, however, between these fluctuating intensities and changes in speed of the bacteria. These measurements suggest that while actin polymerization at the bacterial surface is coupled to the movement of the bacterium, the periodic changes in intracellular motility are not a simple function of the number of actin filaments nucleating at the bacterial surfaces. © 1994 Wiley-Liss, Inc.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
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