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Protein Engineering, Vol 10, 99-101, Copyright © 1997 by Oxford University Press

ARTICLES

Circular dichroism analysis of the interaction between the alpha and beta subunits in a killer toxin produced by a halotolerant yeast, Pichia farinosa

C Suzuki, T Kashiwagi, F Tsuchiya, N Kunishima, K Morikawa, S Nikkuni and Y Arata
National Food Research Institute, Tsukuba-shi, Ibaraki.

SMK toxin is a killer toxin produced by a halotolerant yeast, Pichia farinosa. It is a heterodimer consisting of alpha (63 aa) and beta (77 aa) subunits, between which no disulfide bond exists. The two subunits interact tightly with each other below pH 5. However, the subunits dissociate under neutral conditions, resulting in the aggregation of the alpha subunit and the concomitant loss of killer activity. CD spectral measurements showed that the secondary structure of the SMK toxin changes drastically in the pH range 5.1-5.5 and that after the dissociation of the subunits, the soluble beta subunit alone cannot take any secondary structure. It was also shown that the concentration of NaCl does not affect the secondary structure of the SMK toxin.
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C. Suzuki, M. Kawano, T. Kashiwagi, Y. Arata, T. Kawasumi, and Y. Kashiwagi
Lethal effect of the expression of a killer gene SMK1 in Saccharomyces cerevisiae
Protein Eng. Des. Sel., February 1, 2000; 13(2): 73 - 76.
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