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PMID: 21873984 Published · epublish English Journal Article Research Support, Non-U.S. Gov't

Mechanism of actin filament nucleation by the bacterial effector VopL.

Nature structural & molecular biology ·Vol. 18 ·No. 9 ·2011-08-28 ·Pages 1068-74

Yu B, Cheng HC, Brautigam CA, Tomchick DR, Rosen MK

Abstract

Vibrio parahaemolyticus protein L (VopL) is an actin nucleation factor that induces stress fibers when injected into eukaryotic host cells. VopL contains three N-terminal Wiskott-Aldrich homology 2 (WH2) motifs and a unique VopL C-terminal domain (VCD). We describe crystallographic and biochemical analyses of filament nucleation by VopL. The WH2 element of VopL does not nucleate on its own and requires the VCD for activity. The VCD forms a U-shaped dimer in the crystal, stabilized by a terminal coiled coil. Dimerization of the WH2 motifs contributes strongly to nucleation activity, as do contacts of the VCD to actin. Our data lead to a model in which VopL stabilizes primarily lateral (short-pitch) contacts between actin monomers to create the base of a two-stranded filament. Stabilization of lateral contacts may be a common feature of actin filament nucleation by WH2-based factors.

MeSH Terms
Actin Cytoskeleton/metabolism Actins/chemistry,metabolism Amino Acid Motifs Bacterial Proteins/chemistry,metabolism,physiology Crystallography, X-Ray Dimerization Microfilament Proteins/chemistry,metabolism,physiology Models, Molecular Protein Structure, Tertiary Vibrio parahaemolyticus/metabolism,ultrastructure
Chemicals
Actins Bacterial Proteins Microfilament Proteins
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Yu Bingke
Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas, Texas, USA.
Cheng Hui-Chun
Brautigam Chad A
Tomchick Diana R
Rosen Michael K
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Article Info
Journal
Nature structural & molecular biology
Abbr.
Nat Struct Mol Biol
ISSN
1545-9985
Published
2011-08-28
Epub
2011-00-28
Pages
1068-74
Language
English
Region
United States
NLM ID
101186374
PMCID
PMC3168117
Subset
IM
Grants
Howard Hughes Medical Institute · United States
Databases
PDB
Corrections
CommentIn
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