Heat causes oligomeric disassembly and increases the chaperone activity of small heat shock proteins from sugarcane |
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| Authors: | Ana O. Tiroli-Cepeda Carlos H.I. Ramos |
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| Affiliation: | 1. Faculty of Chemistry, University of Wroc?aw, Joliot-Curie 14, 50–383 Wroc?aw, Poland;2. Department of Animal Physiology and Development, Institute of Experimental Biology, Adam Mickiewicz University, Umultowska 89, 61–614 Poznań, Poland;3. Department of Systematic Zoology, Adam Mickiewicz University, Umultowska 89, 61–614 Poznań, Poland;1. Faculty of Chemistry, University of Wroc?aw, Joliot-Curie 14, 50-383 Wroc?aw, Poland;2. Department of Animal Physiology and Development, Institute of Experimental Biology, Adam Mickiewicz University, Umultowska 89, 61-614 Poznań, Poland;3. Department of Systematic Zoology, Adam Mickiewicz University, Umultowska 89, 61-614 Poznań, Poland |
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| Abstract: | Small heat shock proteins (sHsp) constitute an important chaperone family linked to conformational diseases. In plants, sHsps prevent protein aggregation by acting as thermosensors and to enhance cell stress tolerance. SsHsp17.2 and SsHsp17.9 are the most highly expressed class I sHsps in sugarcane. They exist as dodecamers at 20 °C and have distinct substrate specificities. Therefore, they are useful models to study how class I SHsps work. Here we present data on the effects of heat on the oligomerization and chaperone activity of SsHsp17.2 and SsHsp17.9. Using several biophysical and biochemical probes, we show that the effects of heat are completely reversible, an important property for proteins that act at heat shock temperatures. SsHsp17.2 and SsHsp17.9 dodecamers dissociated to dimers at temperatures ranging from 40 to 45 °C and this dissociation was followed by enhanced chaperone activity. We conclude that high temperature affects the oligomeric state of these chaperones, resulting in enhanced chaperone activity. |
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