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A tormentor in the quest for plant p53-like proteins

Author: Korthout, H.A.A.J · Caspers, M.P.M · Kottenhagen, M.J. · Helmer, Q. · Wang, M.
Institution: Centraal Instituut voor Voedingsonderzoek TNO TNO Voeding
Source:FEBS Letters, 1-3, 526, 53-57
Identifier: 236660
doi: doi:10.1016/S0014-5793(02)03113-7
Keywords: 2-Oxoglutarate dehydrogenase · Barley · Immuno recognition · Pab240 · cross reacting antibody · Epitope · Monoclonal antibody · Monoclonal antibody pab240 · Oxoglutarate dehydrogenase · Protein p53 · Unclassified drug · Vegetable protein · Amino acid sequence · Controlled study · DNA library · DNA screening · DNA sequence · Molecular cloning · Molecular weight · Nonhuman · Protein analysis · Protein degradation · Protein isolation · Protein purification · Sequence analysis · Amino Acid Sequence · Base Sequence · Hordeum · Ketoglutarate Dehydrogenase Complex · Molecular Sequence Data · Plant Proteins · Sequence Alignment · Sequence Homology, Amino Acid · Sequence Homology, Nucleic Acid · Tumor Suppressor Protein p53 · Hordeum vulgare subsp. vulgare


Over the past few years the presence of p53-like proteins in plants was frequently reported, by using the monoclonal antibody Pab240. By means of protein purification and screening a cDNA library, a Pab240 cross-reacting protein and a cDNA clone were isolated from barley. Peptide- and DNA-sequence analysis identified one and the same protein: 2-oxoglutarate dehydrogenase. Sequence analysis of 2-oxoglutarate dehydrogenase revealed that the protein contains a perfect Pab240 epitope. In barley, the 110 kDa oxoglutarate dehydrogenase was degraded during isolation to a 53 kDa Pab240 cross-reacting polypeptide, thereby mimicking curiously p53-like properties. © 2002 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved. Chemicals/CAS: Ketoglutarate Dehydrogenase Complex, EC; Plant Proteins; Tumor Suppressor Protein p53