Premium
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.
Accelerating Research
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom
Address
John Eccles HouseRobert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom