Premium
Both plant and animal LEA proteins act as kinetic stabilisers of polyglutamine‐dependent protein aggregation
Author(s) -
Liu Yun,
Chakrabortee Sohini,
Li Ranhui,
Zheng Yizhi,
Tunnacliffe Alan
Publication year - 2011
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2011.01.020
Subject(s) - protein aggregation , in vitro , recombinant dna , chemistry , function (biology) , microbiology and biotechnology , biochemistry , biology , gene
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.