RT Journal Article
SR Electronic
T1 A widespread family of heat-resistant obscure (Hero) proteins protect against protein instability and aggregation
JF bioRxiv
FD Cold Spring Harbor Laboratory
SP 816124
DO 10.1101/816124
A1 Kotaro Tsuboyama
A1 Tatsuya Osaki
A1 Eriko Suzuki-Matsuura
A1 Hiroko Kozuka-Hata
A1 Yuki Okada
A1 Masaaki Oyama
A1 Yoshiho Ikeuchi
A1 Shintaro Iwasaki
A1 Yukihide Tomari
YR 2019
UL http://biorxiv.org/content/early/2019/11/22/816124.abstract
AB Proteins are typically denatured and aggregated by heat. Exceptions to this principle include highly disordered and heat-resistant proteins found in extremophiles, which help these organisms tolerate extreme conditions such as drying, freezing, and high salinity. In contrast, the functions of heat-soluble proteins in non-extremophilic organisms including humans remain largely unexplored. Here we report that heat-resistant obscure (Hero) proteins, which remain soluble after boiling at 95°C, are widespread in Drosophila and humans. Hero proteins are hydrophilic and highly charged, and function to stabilize various “client” proteins, protecting them from denaturation even under stress conditions such as heat shock, desiccation, and exposure to organic solvents. Hero proteins can also block several different types of pathological protein aggregations in cells and in Drosophila strains that model neurodegenerative diseases. Moreover, Hero proteins can extend lifespan of Drosophila. Our study reveals that organisms naturally use Hero proteins as molecular shields to stabilize protein functions, highlighting their biotechnological and therapeutic potential.