Post-translational Assembly of Lens alpha-Crystallin in the Reticulocyte Lysate and in Xenopus laevis Oocytes

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Abstract
Calf lens mRNA was translated in a 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 X. laevis oocytes, produced .alpha.-crystallin subunits that were exclusively found in the form of high-MW complexes. After injection of the purified 14-S mRNA, coding for the .alpha.A subunit, the synthesized .alpha.A polypeptides were incorporated into high-MW aggregates. In contrast, the synthesis of .alpha.B 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 .alpha.A subunits, which are then joined by the .alpha.B subunits. This process occurs partly in the cell-free system and completely in Xenopus occytes.

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