PMID:20433838

Citation	Ratajczak, E, Strózecka, J, Matuszewska, M, Zietkiewicz, S, Kuczyńska-Wiśnik, D, Laskowska, E and Liberek, K (2010) IbpA the small heat shock protein from Escherichia coli forms fibrils in the absence of its cochaperone IbpB. FEBS Lett. 584:2253-7
Abstract	Small heat shock proteins (sHsps) associate with aggregated proteins, changing their physical properties in such a way that chaperone mediated disaggregation becomes much more efficient. In Escherichia coli two small Hsps, IbpA and IbpB, exist. They are 48% identical at the amino acid level, yet their roles in stabilisation of protein aggregates are quite distinct. Here we analysed the biochemical properties of IbpA. We found that IbpA assembles into protofilaments which in turn form mature fibrils. Such fibrils are atypical for sHsps. Interaction of IbpA with either its cochaperone IbpB or an aggregated substrate blocks IbpA fibril formation.
Links	PubMed Online version:10.1016/j.febslet.2010.04.060
Keywords	Animals; Escherichia coli/chemistry; Escherichia coli/genetics; Escherichia coli/metabolism; Escherichia coli Proteins/genetics; Escherichia coli Proteins/metabolism; Heat-Shock Proteins/genetics; Heat-Shock Proteins/metabolism; Inclusion Bodies/metabolism; Mice; Molecular Chaperones/chemistry; Molecular Chaperones/genetics; Molecular Chaperones/metabolism; Protein Structure, Secondary/genetics
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