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Functional differentiation of small heat shock proteins in diapause‐destined A rtemia embryos
Author(s) -
King Allison M.,
Toxopeus Jantina,
MacRae Thomas H.
Publication year - 2013
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/febs.12442
Subject(s) - embryo , biology , diapause , gene knockdown , microbiology and biotechnology , rna , heat shock protein , rna interference , messenger rna , gene expression , translation (biology) , gene , botany , genetics , larva
Encysted embryos of A rtemia franciscana cease development and enter diapause, a state of metabolic suppression and enhanced stress tolerance. The development of diapause‐destined A rtemia embryos is characterized by the coordinated synthesis of the small heat shock proteins (s H sps) p26, A r H sp21 and A r H sp22, with the latter being stress inducible in adults. The amounts of s H sp m RNA and protein varied in A rtemia cysts, suggesting transcriptional and translational regulation. By contrast to p26, knockdown of A rHsp21 by RNA interference had no effect on embryo development. A r H sp21 provided limited protection against stressors such as desiccation and freezing but not heat. A r H sp21 may have a non‐essential or unidentified role in cysts. Injection of A rtemia adults with amounts of A r H sp22 double‐stranded RNA less than those used for other s H sps killed females and males, curtailing the analysis of A r H sp22 function in developing embryos and cysts. The results indicate that diapause‐destined A rtemia embryos synthesize varying amounts of s H sps as a result of differential gene expression and m RNA translation and also suggest that these s H sps have distinctive functions.