| Literature DB >> 26118535 |
Eunyoung Park1, Brian R Graziano2, Wei Zheng1, Mikael Garabedian2, Bruce L Goode2, Michael J Eck3.
Abstract
In budding yeast, the actin-binding protein Bud6 cooperates with formins Bni1 and Bnr1 to catalyze the assembly of actin filaments. The nucleation-enhancing activity of Bud6 requires both a "core" domain that binds to the formin and a "flank" domain that binds monomeric actin. Here, we describe the structure of the Bud6 flank domain in complex with actin. Two helices in Bud6(flank) interact with actin; one binds in a groove at the barbed end of the actin monomer in a manner closely resembling the helix of WH2 domains, a motif found in many actin nucleation factors. The second helix rises along the face of actin. Mutational analysis verifies the importance of these Bud6-actin contacts for nucleation-enhancing activity. The Bud6 binding site on actin overlaps with that of the formin FH2 domain and is also incompatible with inter-subunit contacts in F-actin, suggesting that Bud6 interacts only transiently with actin monomers during filament nucleation.Entities:
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Year: 2015 PMID： 26118535 PMCID： PMC4578302 DOI： 10.1016/j.str.2015.05.015
Source DB: PubMed Journal: Structure ISSN： 0969-2126 Impact factor: 5.006