Journalartikel

Jahr der Veröffentlichung: 2000

Seiten: 3277-3287

Zeitschrift: Journal of Cell Science

Bandnummer: 113

Heftnummer: 18

ISSN: 0021-9533

eISSN: 1477-9137

Verlag: The Company of Biologists

Abstract: 
The recruitment of actin to the surface of intracellular Listeria monocytogenes and subsequent tail formation is dependent on the expression of the bacterial surface protein ActA, Of the different functional domains of ActA identified thus far, the N-terminal region is absolutely required for actin filament recruitment and intracellular motility, Mutational analysis of this domain which abolished actin recruitment by intracellular Listeria monocytogenes identified two arginine residues within the 146-KKRRK-150 motif that are essential for its activity. More specifically, recruitment of the Arp2/3 complex to the bacterial surface, as assessed by immunofluorescence staining with antibodies raised against the p21-Arc protein, was not obtained in these mutants. Consistently, treatment of infected cells,vith latrunculin B, which abrogated actin filament formation, did not affect association of ActA,vith p21-Arc at the bacterial surface. Thus, the initial recruitment of the Arp2/3 complex to the bacterial surface is independent of, and precedes, actin polymerisation, Our data suggest that binding of the Arp2/3 complex is mediated by specific interactions dependent on arginine residues within the 146-KKRRK-150 motif present in ActA.

Harvard-Zitierstil: Pistor, S., Gröbe, L., Sechi, A., Domann, E., Gerstel, B., Machesky, L., et al. (2000) Mutations of arginine residues within the 146-KKRRK-150 motif of the ActA protein of Listeria monocytogenes abolish intracellular motility by interfering with the recruitment of the Arp2/3 complex, Journal of Cell Science, 113(18), pp. 3277-3287

APA-Zitierstil: Pistor, S., Gröbe, L., Sechi, A., Domann, E., Gerstel, B., Machesky, L., Chakraborty, T., & Wehland, J. (2000). Mutations of arginine residues within the 146-KKRRK-150 motif of the ActA protein of Listeria monocytogenes abolish intracellular motility by interfering with the recruitment of the Arp2/3 complex. Journal of Cell Science. 113(18), 3277-3287.