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J. Biol. Chem., Vol. 275, Issue 37, 28428-28432, September 15, 2000
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From the Groningen Biomolecular Sciences and Biotechnology
Institute, University of Groningen, Nijenborgh 4, NL-9747 AG Groningen, the Netherlands
Hydrophobins function in fungal development by
self-assembly at hydrophobic-hydrophilic interfaces such as the
interface between the fungal cell wall and the air or a hydrophobic
solid. These proteins contain eight conserved cysteine residues that
form four disulfide bonds. To study the effect of the disulfide bridges on the self-assembly, the disulfides of the SC3 hydrophobin were reduced with 1,4-dithiothreitol. The free thiols were then blocked with
either iodoacetic acid (IAA) or iodoacetamide (IAM), introducing eight or zero negative charges, respectively. Circular dichroism and
infrared spectroscopy showed that after opening of the disulfide bridges SC3 is initially unfolded. IAA-SC3 did not self-assemble at the
air-water interface upon shaking an aqueous solution. Remarkably, after
drying down IAA-SC3 or after exposing it to Teflon, it refolded into a
structure similar to that observed for native SC3 at these interfaces.
Iodoacetamide-SC3 on the other hand, which does not contain extra
charges, spontaneously refolded in water in the amyloid-like
Structural and Functional Role of the Disulfide Bridges in the
Hydrophobin SC3*
-sheet
conformation, characteristic for SC3 assembled at the water-air
interface. From this we conclude that the disulfide bridges of SC3 are
not directly involved in self-assembly but keep hydrophobin monomers
soluble in the fungal cell or its aqueous environment, preventing
premature self-assembly.
*
This research was financially supported by the Netherlands
Technology Foundation (Stichting Technisch Wetenschappen) and
was coordinated by the Life Sciences Foundation (Stichting
Levenswetenschappen).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed. Tel.: 00 31 363 4321;
Fax: 00 31 363 4165; E-mail: g.t.robillard@chem.rug.nl.
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