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Protein Science (2004), 13:810-821. Published by Cold Spring Harbor Laboratory Press. Copyright © 2004 The Protein Society
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Oligomerization of hydrophobin SC3 in solution: From soluble state to self-assembly

Xiaoqin Wang1,4, Johanna F. Graveland-Bikker2, Cornelis G. De Kruif2,3 and George T. Robillard1,4

1 BioMaDe Technology Foundation, 9747 AG Groningen, The Netherlands
2 NIZO food research, 6710 BA Ede, The Netherlands
3 Van’t Hoff Laboratory, Debeye Research Institute, Utrecht University, 3584 CH Utrecht, The Netherlands
4 Department of Biochemistry, University of Groningen, 9747 AG Groningen, The Netherlands

(RECEIVED August 13, 2003; FINAL REVISION November 26, 2003; ACCEPTED December 2, 2003)



Abstract

Hydrophobin SC3 is a protein with special self-association properties that differ depending on whether it is in solution, on an air/water interface or on a solid surface. Its self-association on an air/water interface and solid surface have been extensively characterized. The current study focuses on its self-association in water because this is the starting point for the other two association processes. Size-exclusion chromatography was used to fractionate soluble-state SC3. Real-time multiangular light scattering detection of the eluate indicated that SC3 mainly exists as a dimer in buffer, accompanied with a small amount of monomer, tetramer, and larger aggregates. Dimeric SC3 has very likely an elongated shape, as indicated by the hydrodynamic radius determined by using dynamic light scattering (DLS) and fluorescence anisotropy measurements on dansyl-labeled SC3. Size-exclusion chromatography experiments also indicated that the protein oligomerizes very slowly at low temperature (4°C) but rather rapidly at room temperature. Ionic strength plays an important role in the oligomerization; a short-lived monomeric SC3 species could be observed in pure water. Oligomerization was not affected by low pH but was accelerated by high pH. Fluorescence resonance energy transfer showed that dissociation occurred when the protein concentration was lowered; a large population of oligomers, presumably dimers, dissociate when the protein concentration is <4.5 µg/mL. This value is similar to the critical concentration for SC3 self-assembly. Therefore, dimeric SC3 is indicated to be the building block for both aggregation in solution and self-assembly at hydrophobic/hydrophilic interfaces.

Keywords: hydrophobin SC3; oligomerization; molecular exchange; association/dissociation; structural changes; self-assembly

Reprint requests to: George T. Robillard, BioMaDe Technology Foundation, Nijenborgh 4, 9747 AG Groningen, The Netherlands; e-mail: Robillard{at}biomade.nl; fax: 31-50-3634429.

Article and publication are at http://www.proteinscience.org/cgi/doi/10.1110/ps.03367304.


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