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J Struct Biol. 2015 May;190(2):192-9. doi: 10.1016/j.jsb.2015.03.008. Epub 2015 Mar 25.

Dimeric WH2 repeats of VopF sequester actin monomers into non-nucleating linear string conformations: An X-ray scattering study.

Author information

1
Cytoskeleton Dynamics and Motility Group, CNRS, Gif-sur-Yvette, France. Electronic address: balendu.avvaru@gmail.com.
2
Cytoskeleton Dynamics and Motility Group, CNRS, Gif-sur-Yvette, France.
3
Cytoskeleton Dynamics and Motility Group, CNRS, Gif-sur-Yvette, France. Electronic address: carlier@lebs.cnrs-gif.fr.

Abstract

VopF and VopL are highly similar virulence-factors of Vibrio cholerae and Vibrio parahaemolyticus respectively that disrupt the host's actin cytoskeleton, using a unique organization in dimerized WH2 repeats. Association of dimerized WH2 domains with the barbed face of actin confers multifunctional activities to VopF in vitro, including G-actin sequestration and filament nucleation, barbed end tracking and uncapping. Here, small angle X-ray scattering (SAXS) measurements of complexes of VopF with actin and structural modeling reveal that VopF stabilizes linear actin-strings that differ from canonical actin filament architectures but represent non-polymerizable sequestered forms of actin. The results exclude that VopL binds the pointed end of actin filaments in the template filament nucleation mechanism derived from crystallographic studies.

KEYWORDS:

Actin; SAXS; VopF; WH2 domain repeats

PMID:
25818509
DOI:
10.1016/j.jsb.2015.03.008
[Indexed for MEDLINE]

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