ActA is a Dimer

ActA, a surface protein of Listeria monocytogenes, is able to induce continuous actin polymerization at the rear of the bacterium, in the cytosol of the infected cells. Its N-terminal domain is sufficient to induce actin tail formation and movement. Here, we demonstrate, using the yeast two-hybrid s...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 1997-09, Vol.94 (19), p.10034-10039
Main Authors: Mourrain, Philippe, Lasa, Inigo, Gautreau, Alexis, Gouin, Edith, Pugsley, Anthony, Cossart, Pascale
Format: Article
Language:English
Subjects:
Actins
Amino acids
Bacteria
Bacterial Proteins - chemistry
Bacterial Proteins - genetics
Biological Sciences
Cellular biology
Dimerization
Dimers
Ligands
Listeria monocytogenes
Listeria monocytogenes - chemistry
Membrane Proteins - chemistry
Membrane Proteins - genetics
Plasmids
Polymerization
Proteins
Recombinant Proteins - chemistry
Recombinant Proteins - genetics
Saccharomyces cerevisiae - genetics
Yeast
Yeasts
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Summary:ActA, a surface protein of Listeria monocytogenes, is able to induce continuous actin polymerization at the rear of the bacterium, in the cytosol of the infected cells. Its N-terminal domain is sufficient to induce actin tail formation and movement. Here, we demonstrate, using the yeast two-hybrid system, that the N-terminal domain of ActA may form homodimers. By using chemical cross-linking to explore the possibility that ActA could be a multimer on the surface of the bacteria, we show that ActA is a dimer. Cross-linking experiments on various L. monocytogenes strains expressing different ActA variants demonstrated that the region spanning amino acids 97-126, and previously identified as critical for actin tail formation, is also critical for dimer formation. A model of actin polymerization by L. monocytogenes, involving the ActA dimer, is presented.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.94.19.10034