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Issue 6, 2011
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Evaluation of a symmetry-based strategy for assembling protein complexes

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Abstract

We evaluate a strategy for assembling proteins into large cage-like structures, based on the symmetry associated with the native protein's quaternary structure. Using a trimeric protein, KDPG aldolase, as a building block, two fusion proteins were designed that could assemble together upon mixing. The fusion proteins, designated A-(+) and A-(−), comprise the aldolase domain, a short, flexible spacer sequence, and a sequence designed to form a heterodimeric antiparallel coiled-coil between A-(+) and A-(−). The flexible spacer is included to minimize constraints on the ability of the fusion proteins to assemble into larger structures. On incubating together, A-(+) and A-(−) assembled into a mixture of complexes that were analyzed by size exclusion chromatography coupled to multi-angle laser light scattering, analytical ultracentrifugation, transmission electron microscopy and atomic force microscopy. Our analysis indicates that, despite the inherent flexibility of the assembly strategy, the proteins assemble into a limited number of globular structures. Dimeric and tetrameric complexes of A-(+) and A-(−) predominate, with some evidence for the formation of larger assemblies; e.g. octameric A-(+) : A-(−) complexes.

Graphical abstract: Evaluation of a symmetry-based strategy for assembling protein complexes

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Article information


Submitted
07 Jun 2011
Accepted
11 Aug 2011
First published
20 Sep 2011

RSC Adv., 2011,1, 1004-1012
Article type
Paper

Evaluation of a symmetry-based strategy for assembling protein complexes

D. P. Patterson, A. M. Desai, M. M. B. Holl and E. N. G. Marsh, RSC Adv., 2011, 1, 1004
DOI: 10.1039/C1RA00282A

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