Post-translational assembly of lens alpha-crystallin in the reticulocyte lysate and in Xenopus laevis oocytes.

Lens mRNA was translated in reticulocyte lysate predominantly into monomeric alpha-crystallin chains. Lens polyribosomes added to the cell-free system produced the same polypeptides, but these were detected predominantly in alpha-crystallin aggregates. Lens mRNA, after microinjection into Xenopus laevis oocytes, produced alpha-crystallin subunits that were exclusively found in the form of high-molecular-weight complexes. Also after injection of the purified 14-S mRNA, coding for the alphaA subuint, the synthesized alpha-A polypeptides were incorporated into high-molecular-weight aggregates. In contrast, the synthesis of alphaB subunits, directed by a 10-S mRNA, did not result in aggregate formation. The experiments thus suggest that aggregate formation of alpha-crystallin is triggered by its alphaA subunits, which are then joined by the alphaB subunits. This process occurs partly in the cell-free system and completely in Xenopus oocytes.