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 reg...

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Bibliographic Details
Published in:	Biochimica et biophysica acta Vol. 1263; no. 1; p. 79
Main Authors:	Liebich, I, Voigt, J
Format:	Journal Article
Language:	English
Published:	Netherlands 25-07-1995
Subjects:	14-3-3 Proteins Amino Acid Sequence Animals Base Sequence Binding Sites Chlamydomonas reinhardtii - genetics DNA, Complementary - chemistry DNA, Complementary - isolation & purification Molecular Sequence Data Phylogeny Proteins - chemistry Proteins - genetics Sequence Alignment Tyrosine 3-Monooxygenase
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Summary:	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.
ISSN:	0006-3002