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Both plant and animal LEA proteins act as kinetic stabilisers of polyglutamine-dependent protein aggregation
Authors:Liu Yun  Chakrabortee Sohini  Li Ranhui  Zheng Yizhi  Tunnacliffe Alan
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
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.
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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