Translational activation of maternal mRNA encoding the heat-shock protein hsp90 during sea urchin embryogenesis.

Changes in protein synthesis induced by heat shock of Strongylocentrotus purpuratus gastrulae were analyzed bt two-dimensional electrophoresis. Hyperthermia induces the synthesis of polypeptides having molecular masses of 90, 70, 50, 40, and 38 kDa. One of these, hsp90, appears as a pair of polypeptides which comigrates with proteins synthesized at normal temperature in eggs and embryos; these comigrating spots produce indistinguishable patterns upon electrophoretic analysis of partial V8 protease digests, indicating that hsp90 is synthesized throughout embryogenesis. The relative rate of incorporation of methionine into hsp90 is low in eggs and zygotes, but increases abruptly in morulae, constituting a rare and striking change in protein synthesis during early development. Cell-free translation analyses indicate that most of the mRNA encoding hsp90 resides in the pool of free ribonucleoprotein particles in eggs and early embryos, but shifts to polysomes by the 64-cell stage while remaining constant in mass. Thus the increase in synthesis of hsp90 appears to be via the selective activation of translation of a stored maternal mRNA. The shift of hsp90 mRNA to polysomes is accompanied by polyadenylation. Heat shock of eggs or zygotes did not result in translational activation of hsp90 mRNA. The sea urchin hsp90 doublet of spots comigrates with hsp90 induced by heat shock of chicken embryo fibroblasts, a conserved protein abundant in many cells of a variety of species.