Translation in vitro of Tetrahymena pyriformis Polyadenylated mRNA

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Abstract
The capacity of poly(A)-containing RNA of the protozoan ciliate T. pyriformis to direct the synthesis of proteins in vitro was tested using 2 cell-free systems: a wheat germ extract and a rabbit reticulocyte lysate. Results obtained with the 2 systems were compared and the identification of .alpha. and .beta. tubulins among the products of protein synthesis in vitro after separation by 1-dimensional and 2-dimensional electrophoresis is described. By isoelectric focusing in polyacrylamide gels, each species of tubulin is resolved into several bands, suggesting that the main subunits are more heterogeneous than has been generally described. Poly(A)-containing RNA was also fractionated on a 70% formamide/sucrose gradient showing that .alpha. and .beta. tubulins are coded by separate mRNA.