A Chlamydomonas homologue to the 14-3-3 proteins: cDNA and deduced amino acid sequence

Biochim Biophys Acta. 1995 Jul 25;1263(1):79-85. doi: 10.1016/0167-4781(95)00097-z.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • 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*

Substances

  • 14-3-3 Proteins
  • DNA, Complementary
  • Proteins
  • Tyrosine 3-Monooxygenase

Associated data

  • GENBANK/D17615
  • GENBANK/L09110
  • GENBANK/L09112
  • GENBANK/L29150
  • GENBANK/L29151
  • GENBANK/M05038
  • GENBANK/M09376
  • GENBANK/M84416
  • GENBANK/M96855
  • GENBANK/P34730
  • GENBANK/X79445
  • GENBANK/Z19599