Structural characterization of the hydrophobin SC3, as a monomer and after self-assembly at hydrophobic/hydrophilic interfaces

被引:151
作者
de Vocht, ML
Scholtmeijer, K
van der Vegte, EW
de Vries, OMH
Sonveaux, N
Wösten, HAB
Ruysschaert, JM
Hadziioannou, G
Wessels, JGH
Robillard, GT
机构
[1] Univ Groningen, Groningen Biomol Sci & Biotechnol Inst, NL-9747 AG Groningen, Netherlands
[2] Univ Groningen, Dept Biochem, NL-9747 AG Groningen, Netherlands
[3] Univ Groningen, Dept Plant Biol, NL-9747 AG Groningen, Netherlands
[4] Univ Groningen, Dept Polymer Chem, NL-9747 AG Groningen, Netherlands
[5] Univ Groningen, Ctr Mat Sci, NL-9747 AG Groningen, Netherlands
[6] Free Univ Brussels, Chim Phys Macromol Interfaces Lab, Brussels, Belgium
关键词
D O I
10.1016/S0006-3495(98)77912-3
中图分类号
Q6 [生物物理学];
学科分类号
071011 ;
摘要
Hydrophobins are small fungal proteins that self-assemble at hydrophilic/hydrophobic interfaces into amphipathic membranes that, in the case of Class I hydrophobins, can be disassembled only by treatment with agents like pure trifluoroacetic acid. Here we characterize, by spectroscopic techniques, the structural changes that occur upon assembly at an air/water interface and upon assembly on a hydrophobic solid surface, and the influence of deglycosylation on these events. We determined that the hydrophobin SC3 from Schizophyllum commune contains 16-22 O-linked mannose residues, probably attached to the N-terminal part of the peptide chain. Scanning force microscopy revealed that SC3 adsorbs specifically to a hydrophobic surface and cannot be removed by heating at 100 degrees C in 2% sodium dodecyl sulfate. Attenuated total reflection Fourier transform infrared spectroscopy and circular dichroism spectroscopy revealed that the monomeric, water-soluble form of the protein is rich in beta-sheet structure and that the amount of beta-sheet is increased after self-assembly on a water-air interface. alpha-Helix is induced specifically upon assembly of the protein on a hydrophobic solid. We propose a model for the formation of rodlets, which may be induced by dehydration and a conformational change of the glycosylated part of the protein, resulting in the formation of an amphipathic alpha-helix that forms an anchor for binding to a substrate. The assembly in the beta-sheet form seems to be involved in lowering of the surface tension, a potential function of hydrophobins.
引用
收藏
页码:2059 / 2068
页数:10
相关论文
共 48 条
[1]   Expression of two closely linked hydrophobin genes of Coprinus cinereus is monokaryon-specific and down-regulated by the oid-1 mutation [J].
Asgeirsdottir, SA ;
Halsall, JR ;
Casselton, LA .
FUNGAL GENETICS AND BIOLOGY, 1997, 22 (01) :54-63
[2]  
ASGEIRSDOTTIR SA, 1994, THESIS U GRONINGEN G
[3]   FORMATION OF MONOLAYER FILMS BY THE SPONTANEOUS ASSEMBLY OF ORGANIC THIOLS FROM SOLUTION ONTO GOLD [J].
BAIN, CD ;
TROUGHTON, EB ;
TAO, YT ;
EVALL, J ;
WHITESIDES, GM ;
NUZZO, RG .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1989, 111 (01) :321-335
[4]  
BATY AM, 1996, J COLLOID INTERF SCI, V177, P37
[5]   INTERFACIAL ADSORPTION AND AGGREGATION ASSOCIATED CHANGES IN SECONDARY - STRUCTURE OF HUMAN CALCITONIN MONITORED BY ATR-FTIR SPECTROSCOPY [J].
BAUER, HH ;
MULLER, M ;
GOETTE, J ;
MERKLE, HP ;
FRINGELI, UP .
BIOCHEMISTRY, 1994, 33 (40) :12276-12282
[6]   CIRCULAR DICHROIC ANALYSIS OF PROTEIN CONFORMATION - INCLUSION OF BETA-TURNS [J].
CHANG, CT ;
WU, CSC ;
YANG, JT .
ANALYTICAL BIOCHEMISTRY, 1978, 91 (01) :13-31
[7]   INSOLUBLE HYDROPHOBIN COMPLEXES IN THE WALLS OF SCHIZOPHYLLUM-COMMUNE AND OTHER FILAMENTOUS FUNGI [J].
DEVRIES, OMH ;
FEKKES, MP ;
WOSTEN, HAB ;
WESSELS, JGH .
ARCHIVES OF MICROBIOLOGY, 1993, 159 (04) :330-335
[8]   DEGLYCOSYLATION OF GLYCOPROTEINS BY TRIFLUOROMETHANESULFONIC ACID [J].
EDGE, ASB ;
FALTYNEK, CR ;
HOF, L ;
REICHERT, LE ;
WEBER, P .
ANALYTICAL BIOCHEMISTRY, 1981, 118 (01) :131-137
[9]  
Fairbairn N.J., 1953, CHEM IND, V4, P86
[10]   FUNCTIONAL-GROUP IMAGING BY CHEMICAL FORCE MICROSCOPY [J].
FRISBIE, CD ;
ROZSNYAI, LF ;
NOY, A ;
WRIGHTON, MS ;
LIEBER, CM .
SCIENCE, 1994, 265 (5181) :2071-2074