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
| Autor: | Jürgen Wehland, Laura M. Machesky, Eugen Domann, Trinad Chakraborty, Antonio Sechi, Susanne Pistor, Birgit Gerstel, Lothar Gröbe |
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| Rok vydání: | 2000 |
| Předmět: |
Intracellular Fluid
Arginine Amino Acid Motifs Molecular Sequence Data Mutant Motility Arp2/3 complex macromolecular substances Biology medicine.disease_cause Cell Line Bacterial Proteins Listeria monocytogenes medicine Animals Point Mutation Amino Acid Sequence Actin Sequence Deletion Cell Membrane Membrane Proteins Biological Transport Cell Biology Chromosomes Bacterial Bridged Bicyclo Compounds Heterocyclic Molecular biology Actins Cell biology Cytoskeletal Proteins Thiazoles Genes Bacterial Actin-Related Protein 3 Paracytophagy Actin-Related Protein 2 Mutagenesis Site-Directed biology.protein Thiazolidines Intracellular |
| Zdroj: | Scopus-Elsevier |
| ISSN: | 1477-9137 0021-9533 |
| Popis: | 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 with latrunculin B, which abrogated actin filament formation, did not affect association of ActA with 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. |
| Databáze: | OpenAIRE |
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