IbpA the small heat shock protein from Escherichia coli forms fibrils in the absence of its cochaperone IbpB |
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| Authors: | El?bieta Ratajczak Marlena Matuszewska Dorota Kuczyńska-Wi?nik Krzysztof Liberek |
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| Institution: | a Department of Molecular and Cellular Biology, Intercollegiate Faculty of Biotechnology, 80-822 Gdańsk, Kladki 24, Poland
b Department of Biochemistry, University of Gdańsk, 80-822 Gdańsk, Kladki 24, Poland |
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| 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.Structured summaryMINT-7876715: ibpA (uniprotkb:P0C054) and ibpA (uniprotkb:P0C054) bind (MI:0407) by molecular sieving (MI:0071)MINT-7888427: ibpB (uniprotkb:P0C058) and ibpB (uniprotkb:P0C058) bind (MI:0407) by molecular sieving (MI:0071)MINT-7888448: ibpA (uniprotkb:P0C054) and ibpA (uniprotkb:P0C054) bind (MI:0407) by electron microscopy (MI:0040)MINT-7888434: ibpB (uniprotkb:P0C058) and ibpB (uniprotkb:P0C058) bind (MI:0407) by electron microscopy (MI:0040)MINT-7888459: ibpA (uniprotkb:P0C054) and ibpA (uniprotkb:P0C054) bind (MI:0407) by fluorescence microscopy (MI:0416) |
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| Keywords: | Small heat shock protein Protein aggregation Protein disaggregation Fibril formation |
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