The structural stability and chaperone activity of artemin, a ferritin homologue from diapause-destined Artemia embryos, depend on different cysteine residues.

Diapause-destined embryos of the crustacean, Artemia franciscana, accumulate large amounts of an oligomeric, heat-stable, molecular chaperone termed artemin, a cysteine-enriched ferritin homologue. In this study, cysteines 22, 61, 166, and 172 of artemin were substituted with alanines, respectively yielding ArtC22A, ArtC61A, ArtC166A, and ArtC172A. Wild-type and modified artemins were synthesized in transformed bacteria and purified.

Diversity, structure, and expression of the gene for p26, a small heat shock protein from Artemia.

p26, a small heat shock protein, is thought to protect Artemia embryos from stress during encystment and diapause. Full-length p26 cDNAs were compared and used to determine phylogenetic relationships between several Artemia species. The alpha-crystallin domain of p26 was the most conserved region of the protein and p26 from each Artemia species contained characteristic amino-terminal WD/EPF and carboxy-terminal VPI motifs.

Structural and functional roles for beta-strand 7 in the alpha-crystallin domain of p26, a polydisperse small heat shock protein from Artemia franciscana.

Oviparous development in the extremophile crustacean, Artemia franciscana, generates encysted embryos which enter a profound state of dormancy, termed diapause. Encystment is marked by the synthesis of p26, a polydisperse small heat shock protein thought to protect embryos from stress. In order to elucidate structural/functional relationships within p26 and other polydisperse small heat shock proteins, and to better define the protein's role during diapause, amino acid substitutions R110G, F112R, R114A and Y116D were generated within the p26 alpha-crystallin domain by site-directed mutagenesis.