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Protein Science (2001), 10:2093-2101.
Copyright © 2001 The Protein Society

Multistep nucleus formation and a separate subunit contribution of the amyloidgenesis of heat-denatured monellin

Takashi Konno

Department of Physiology, Fukui Medical University, Yoshida, Fukui 910-1193, Japan

Reprint requests to: Takashi Konno, Department of Physiology, Fukui Medical University, Yoshida, Fukui 910-1193, Japan; e-mail: konno{at}fmsrsa.fukui-med.ac.jp; fax: 81-776-61-8101.

Monellin (MN) is a sweet-tasting plant protein known to form fibrous aggregates in the heat-denatured state. Here the amyloid-type aggregation process of MN is extensively characterized. The amyloidgenesis was initiated in a highly denatured state of MN. A seeding effect of skipping a lag phase of the amyloid formation kinetics established a nucleation-dependent aggregation mechanism. A finely controlled experimental protocol revealed an additional prenucleus stage preceding the maturation of the nucleus, indicating that the initial lag phase is composed of multiple conformational events. The results obtained for the aggregation properties of the separate A and B subunit chains of MN and a recombinant single-chain MN suggest that the B chain exclusively contributed to the amyloid-type aggregation. These findings suggest a scheme for the amyloidgenesis of MN and their subunits, and provide a unique model of amyloidgenesis that is regulated by the subunit composition of protein.

Keywords: Monellin; amyloid; nucleation; seeding effect

Abbreviations: MN, monellin • ThT, thioflavin T • CR, Congo red • CD, circular dichroism • TEM, transmission electron microscopy • SAXS, solution X-ray scattering • Trp, tryptophan • IR, infrared • SMN, a recombinant single-chain monellin


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