A Chlamydomonas homologue to the 14-3-3 proteins: cDNA and deduced amino acid sequence.
We have isolated and sequenced a 1464 bp cDNA from the unicellular green alga Chlamydomonas reinhardtii encoding an acidic polypeptide (259 aa) with considerable homologies to the 14-3-3 proteins of animals, yeasts and higher plants. Like the other members of this highly conserved protein kinase regulatory protein family, the deduced amino acid sequence of the Chlamydomonas 14-3-3 protein includes two putative phosphorylation sites within the N-terminal region (positions 62 and 67). Furthermore, an EF hand motif characteristic for Ca(2+)-binding sites is located within the C-terminal part of this polypeptide (positions 208-219). EF hand motifs are also present in the 14-3-3 proteins of some higher plants but not in those of animals and yeasts.
Liebich
I
I
Botanisches Institut, Technische Universität Braunschweig, Germany.
Voigt
J
J
D048948:14-3-3 Proteins; D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D001665:Binding Sites; D016825:Chlamydomonas reinhardtii / Q000235:genetics*; D018076:DNA, Complementary / Q000737:chemistry / Q000302:isolation & purification*; D008969:Molecular Sequence Data; D010802:Phylogeny; D011506:Proteins / Q000737:chemistry / Q000235:genetics*; D016415:Sequence Alignment; D014446:Tyrosine 3-Monooxygenase
D048948:14-3-3 Proteins; D018076:DNA, Complementary; D011506:Proteins; D014446:Tyrosine 3-Monooxygenase