Mechanism and application of molecular self-assembly in Sup35 prion domain of Saccharomyces cerevisiae.
- Author:
Wen YIN
1
;
Jin HE
;
Ziniu YU
;
Jieping WANG
Author Information
1. State Key Laboratory ofAgricultural Microbiology, National Engineering Research Center of Microbial Pesticides, Huazhong Agricultural University, Wuhan 430070, China.
- Publication Type:Journal Article
- MeSH:
Amino Acid Sequence;
Amyloid;
chemistry;
metabolism;
Molecular Sequence Data;
Peptide Termination Factors;
chemistry;
Prions;
chemistry;
Protein Conformation;
Saccharomyces cerevisiae;
genetics;
metabolism;
Saccharomyces cerevisiae Proteins;
chemistry
- From:
Chinese Journal of Biotechnology
2011;27(10):1401-1407
- CountryChina
- Language:Chinese
-
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.
