Fig. 1: The tardigrade Hypsibius exemplaris has nine small heat shock proteins, several of which are highly expressed.
From: Tardigrade small heat shock proteins can limit desiccation-induced protein aggregation
a Nine sHSPs were identified that conform to the typical structure containing an alpha-crystallin domain flanked by disordered N-terminal and C-terminal domains. b Seven of nine sHSPs were upregulated during desiccation in RNA-seq data from Boothby et al. 2017 (HSP17, HSP19, HSP20, HSP21, HSP23, HSP24.6, and HSP38, FDR < 0.01). sHSP transcripts are highlighted on a plot of expression fold-change compared to relative abundance from mRNA-seq. c Only one sHSP (HSP23) was significantly upregulated during desiccation (FDR < 0.01) in RNA-seq data from Yoshida et al. 2017.
