A plant homologue to mammalian brain 14-3-3 protein and protein kinase C inhibitor.
We have isolated cDNA clones of Spinacea oleracea L. and Oenothera hookeri of 930 and 1017 base pairs, respectively. The open reading frame deduced from the Oenothera sequence codes for a protein of a calculated molecular mass of 29,200. The primary amino acid sequence exhibits a very high degree (88%) of homology to the 14-3-3 protein from bovine brain, and protein kinase C inhibitor from sheep brain. Subsequently the plant protein was partially purified from leaf extract. The partially purified plant protein inhibited protein kinase C from sheep brain in a heterologous assay system. The active fraction consisted of 5-6 different polypeptides of similar molecular size. One of these proteins crossreacted with a peptide-specific antibody against protein kinase C inhibitor protein from sheep brain.
Hirsch
S
S
Botanisches Institut, Universität Kiel, Germany.
Aitken
A
A
Bertsch
U
U
Soll
J
J
D048948:14-3-3 Proteins; D000595:Amino Acid Sequence; D001483:Base Sequence; D003001:Cloning, Molecular; D008969:Molecular Sequence Data; D009419:Nerve Tissue Proteins / Q000235:genetics* / Q000276:immunology; D010940:Plant Proteins / Q000235:genetics* / Q000276:immunology; D010944:Plants / Q000235:genetics* / Q000276:immunology; D012689:Sequence Homology, Nucleic Acid; D014446:Tyrosine 3-Monooxygenase
D048948:14-3-3 Proteins; D009419:Nerve Tissue Proteins; D010940:Plant Proteins; D014446:Tyrosine 3-Monooxygenase