Chemotaxis of the unicellular green alga Dunaliella salina and the ciliated Tetrahymena pyriformis--effects of glycine, lysine, and alanine, and their oligopeptides.

Chemotactic properties of amino acids (L-alanine, glycine and L-lysine) and their oligopeptides (10(-6) M) and binding sites to these ligands were investigated in two unicellular models, the heterotrophic Tetrahymena pyriformis and the auxotrophic Dunaliella salina. Chemotaxis of Dunaliella induced by simple amino acids and their derivatives demonstrated that binding sites (receptors) for food molecules are not only present in the membrane but are also able to induce their basic physiological response. In Tetrahymena, substances with special molecular structure and properties (polar, hydrophilic character of the signal peptide chain)-5-L-Lys, 5-Gly- were required for chemoattraction, other peptides tested, lacking the required structure, were repellent. Divergences in chemotaxis and binding assays of both species suggest that trends of functional and binding parameters do not run parallel at this level of evolution.