A CHLAMYDOMONAS HOMOLOG TO THE 14-3-3-PROTEINS - CDNA AND DEDUCED AMINO-ACID-SEQUENCE

We have isolated and sequenced a 1464 bp cDNA from the unicellular gre en alga Chlamydomonas reinhardtii encoding an acidic polypeptide (259 aa) with considerable homologies to the 14-3-3 proteins of animals, ye asts and higher plants. Like the other members of this highly conserve d protein kinase regulatory protein family, the deduced amino acid seq uence of the Chlamydomonas 14-3-3 protein includes two putative phosph orylation sites within the N-terminal region (positions 62 and 67). Fu rthermore, an EF hand motif characteristic for Ca2+-binding sites is l ocated within the C-terminal part of this polypeptide (positions 208-2 19). EF hand motifs are also present in the 14-3-3 proteins of some hi gher plants but not in those of animals and yeasts.