title: Small heat shock protein AgsA forms dynamic fibrils.
abstract: As a class of molecular chaperones, small heat shock proteins (sHsps) usually exist as multi-subunit spherical oligomers. In this study, we report that AgsA, a sHsp of Salmonella enterica serovar Typhimurium, spontaneously forms fibrils in vitro. These fibrils tend to be formed at elevated temperature and do not share the characteristics of amyloid. Interestingly, the fibril-forming AgsA is able to suppress the dithiothreitol-induced aggregation of insulin efficiently within a certain range of temperature. During this process, AgsA fibrils disappear and spherical complexes form between AgsA and insulin molecules. These data suggest that AgsA fibrils may represent a distinctive type of structural and functional form of sHsp from spherical oligomers. Our study provides new insights into sHsp structures and chaperone functions.
authors: School of Life Sciences, State Key Laboratory of Protein and Plant Gene Research, Peking University, Beijing 100871, China.
authors: Xiaodong
authors: X
authors: Shi
authors: Zhao
authors: Z
authors: Wang
authors: Linxuan
authors: L
authors: Yan
authors: Anastasia N
authors: AN
authors: Ezemaduka
authors: Guizhen
authors: G
authors: Fan
authors: Rui
authors: R
authors: Wang
authors: Xinmiao
authors: X
authors: Fu
authors: Changcheng
authors: C
authors: Yin
authors: Zengyi
authors: Z
authors: Chang
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism*; D004229:Dithiothreitol / Q000494:pharmacology; D050888:Heat-Shock Proteins, Small / Q000737:chemistry* / Q000378:metabolism*; D007328:Insulin / Q000737:chemistry / Q000378:metabolism; D008854:Microscopy, Electron; D055503:Protein Multimerization; D020836:Protein Structure, Quaternary; D019779:Salmonella enterica; D013696:Temperature
chemical_list: D001426:Bacterial Proteins; D050888:Heat-Shock Proteins, Small; D007328:Insulin; D004229:Dithiothreitol