Journal Article

PreJuSER-19044

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Remodeling of actin filaments by ADF/cofilin proteins

Galkin, V. E. ; Orlova, A. ; Kudryashov, D. S. ; Solodukhin, A. ; Reisler, E. ; Schröder, G. F.FZJ* ; Egelman, E. H.

2011
Academy Washington, DC

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Please use a persistent id in citations: doi:10.1073/pnas.1110109108

Abstract: Cofilin/ADF proteins play key roles in the dynamics of actin, one of the most abundant and highly conserved eukaryotic proteins. We used cryoelectron microscopy to generate a 9-Å resolution three-dimensional reconstruction of cofilin-decorated actin filaments, the highest resolution achieved for a complex of F-actin with an actin-binding protein. We show that the cofilin-induced change in the filament twist is due to a unique conformation of the actin molecule unrelated to any previously observed state. The changes between the actin protomer in naked F-actin and in the actin-cofilin filament are greater than the conformational changes between G- and F-actin. Our results show the structural plasticity of actin, suggest that other actin-binding proteins may also induce large but different conformational changes, and show that F-actin cannot be described by a single molecular model.

Keyword(s): Actin Depolymerizing Factors: chemistry (MeSH) ; Actins: chemistry (MeSH) ; Cofilin 2: chemistry (MeSH) ; Cryoelectron Microscopy: methods (MeSH) ; Cytoskeleton: chemistry (MeSH) ; Gene Library (MeSH) ; Humans (MeSH) ; Microscopy, Electron: methods (MeSH) ; Models, Molecular (MeSH) ; Molecular Conformation (MeSH) ; Muscle, Skeletal: metabolism (MeSH) ; Polymers: chemistry (MeSH) ; Protein Conformation (MeSH) ; Protein Structure, Secondary (MeSH) ; Actin Depolymerizing Factors ; Actins ; Cofilin 2 ; Polymers ; J ; cytoskeleton (auto) ; electron microscopy (auto) ; helical polymers (auto)

Note: This work was supported by National Institutes of Health Grants GM081303 (E. H. E.) and GM077190 (E.R.).

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Contributing Institute(s):

1. Strukturbiochemie (ICS-6)

Research Program(s):

1. Funktion und Dysfunktion des Nervensystems (P33)
2. BioSoft: Makromolekulare Systeme und biologische Informationsverarbeitung (P45)

Appears in the scientific report 2011

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