title: Fibrillogenic propensity of the GroEL apical domain: a Janus-faced minichaperone.
abstract: The chaperonin GroEL plays an essential role in promoting protein folding and in protecting against misfolding and aggregation in the cellular environment. In this study, we report that both GroEL and its isolated apical domain form amyloid-like fibrils under physiological conditions, and that the fibrillation of the apical domain is accelerated under acidic conditions. We also found, however, that despite its fibrillation propensity, the apical domain exhibits a pronounced inhibitory effect on the fibril growth of β(2)-microglobulin. Thus, the analysis of the behaviour of the apical domain reveals how aggregation and chaperone-mediated anti-aggregation processes can be closely related.
authors.affiliation: Okazaki Institute for Integrative Bioscience and Institute for Molecular Science, National Institutes of Natural Sciences, Myodaiji, Okazaki, Japan. jinchen@ims.ac.jp
authors.forename: Jin
authors.initials: J
authors.lastname: Chen
authors.forename: Hisashi
authors.initials: H
authors.lastname: Yagi
authors.forename: Pietro
authors.initials: P
authors.lastname: Sormanni
authors.forename: Michele
authors.initials: M
authors.lastname: Vendruscolo
authors.forename: Koki
authors.initials: K
authors.lastname: Makabe
authors.forename: Takashi
authors.initials: T
authors.lastname: Nakamura
authors.forename: Yuji
authors.initials: Y
authors.lastname: Goto
authors.forename: Kunihiro
authors.initials: K
authors.lastname: Kuwajima
mesh_terms: D000682:Amyloid / Q000378:metabolism*; D001665:Binding Sites; D018834:Chaperonin 60 / Q000737:chemistry* / Q000378:metabolism; D002942:Circular Dichroism; D006801:Humans; D008958:Models, Molecular; D011487:Protein Conformation; D017510:Protein Folding; D001613:beta 2-Microglobulin / Q000737:chemistry / Q000378:metabolism
chemical_list: D000682:Amyloid; D018834:Chaperonin 60; D001613:beta 2-Microglobulin