Both plant and animal LEA proteins act as kinetic stabilisers of polyglutamine-dependent protein aggregation.
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.
School of Life Science, Shenzhen University, Shenzhen City, Guangdong Province, PR China.
Yun
Y
Liu
Sohini
S
Chakrabortee
Ranhui
R
Li
Yizhi
Y
Zheng
Alan
A
Tunnacliffe
D020816:Amino Acid Motifs; D000818:Animals; D052160:Benzothiazoles; D002460:Cell Line; D005456:Fluorescent Dyes; D015801:Helminth Proteins / Q000235:genetics / Q000378:metabolism*; D006706:Homeostasis; D006801:Humans; D007700:Kinetics; D018613:Microscopy, Confocal; D008856:Microscopy, Fluorescence; D018832:Molecular Chaperones / Q000235:genetics / Q000378:metabolism*; D010455:Peptides / Q000378:metabolism*; D010940:Plant Proteins / Q000235:genetics / Q000378:metabolism*; D017510:Protein Folding; D011993:Recombinant Fusion Proteins / Q000378:metabolism; D013844:Thiazoles / Q000378:metabolism; D014908:Triticum / Q000378:metabolism; D017187:Tylenchida / Q000378:metabolism
D052160:Benzothiazoles; C073988:Em protein, Triticum aestivum; D005456:Fluorescent Dyes; D015801:Helminth Proteins; D018832:Molecular Chaperones; D010455:Peptides; D010940:Plant Proteins; D011993:Recombinant Fusion Proteins; D013844:Thiazoles; C066246:late embryogenesis abundant protein, plant; C009462:thioflavin T; C097188:polyglutamine