title: [Mechanism and application of molecular self-assembly in Sup35 prion domain of Saccharomyces cerevisiae].
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.
authors.affiliation: State Key Laboratory ofAgricultural Microbiology, National Engineering Research Center of Microbial Pesticides, Huazhong Agricultural University, Wuhan 430070, China.
authors.forename: Wen
authors.initials: W
authors.lastname: Yin
authors.forename: Jin
authors.initials: J
authors.lastname: He
authors.forename: Ziniu
authors.initials: Z
authors.lastname: Yu
authors.forename: Jieping
authors.initials: J
authors.lastname: Wang
mesh_terms: D000595:Amino Acid Sequence; D000682:Amyloid / Q000737:chemistry* / Q000378:metabolism; D008969:Molecular Sequence Data; D010454:Peptide Termination Factors / Q000737:chemistry*; D011328:Prions / Q000737:chemistry*; D011487:Protein Conformation; D012441:Saccharomyces cerevisiae / Q000235:genetics / Q000378:metabolism*; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry*
chemical_list: D000682:Amyloid; D010454:Peptide Termination Factors; D011328:Prions; C068068:SUP35 protein, S cerevisiae; D029701:Saccharomyces cerevisiae Proteins