Both plant and animal LEA proteins act as kinetic stabilisers of polyglutamine-dependent protein aggregation |
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Authors: | Liu Yun Chakrabortee Sohini Li Ranhui Zheng Yizhi Tunnacliffe Alan |
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Affiliation: | aSchool of Life Science, Shenzhen University, Nanhai Ave 3688, Shenzhen City, Guangdong Province, 518060, PR China;bDepartment of Chemical Engineering and Biotechnology, University of Cambridge, Tennis Court Road, Cambridge CB2 1QT, UK |
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Abstract: | LEA (late embryogenesis abundant) proteins are intrinsically disordered proteins that contribute to stress tolerance in plants and invertebrates. Here we show that, when both plant and animal LEA proteins are co-expressed in mammalian cells with self-aggregating polyglutamine (polyQ) proteins, they reduce aggregation in a time-dependent fashion, showing more protection at early time points. A similar effect was also observed in vitro, where recombinant LEA proteins were able to slow the rate of polyQ aggregation, but not abolish it altogether. Thus, LEA proteins act as kinetic stabilisers of aggregating proteins, a novel function in protein homeostasis consistent with a proposed role as molecular shields. |
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Keywords: | Abbreviations: LEA late embryogenesis abundant PBS phosphate-buffered saline IDP intrinsically disordered protein EGFP enhanced green fluorescent protein GST glutathione transferase ThT thioflavin T polyQ polyglutamine FRET Fö rster resonance energy transfer DAPI 4&prime 6-diamidino-2-phenylindole |
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