Reference: Yin W, et al. (2011) [Mechanism and application of molecular self-assembly in Sup35 prion domain of Saccharomyces cerevisiae]. Sheng Wu Gong Cheng Xue Bao 27(10):1401-7

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Abstract


Sup35 in its native state is a translation termination factor in Saccharomyces cerevisiae. The prion domain of Sup35p can form amyloid-like proteinaceous fibrils in vitro and in vivo. Furthermore, the in-register cross beta-sheet structure of Sup35p amyloid fibrils is similar to those formed in other species. Therefore, studies on mechanism of Sup35p self-assembly can be an appropriate model to study protein misfolding-related diseases and prion biology. Because of its ability to self-assemble into nanowires, the prion domain of Sup35p has been widely used in biotechnology and nanotechnology.

Reference Type
Journal Article | Research Support, Non-U.S. Gov't | Review
Authors
Yin W, He J, Yu Z, Wang J
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