A tormentor in the quest for plant p53-like proteins
article
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 1.2.4.2; Plant Proteins; Tumor Suppressor Protein p53
Topics
2-Oxoglutarate dehydrogenaseBarleyImmuno recognitionPab240cross reacting antibodyEpitopeMonoclonal antibodyMonoclonal antibody pab240Oxoglutarate dehydrogenaseProtein p53Unclassified drugVegetable proteinAmino acid sequenceControlled studyDNA libraryDNA screeningDNA sequenceMolecular cloningMolecular weightNonhumanProtein analysisProtein degradationProtein isolationProtein purificationSequence analysisAmino Acid SequenceBase SequenceHordeumKetoglutarate Dehydrogenase ComplexMolecular Sequence DataPlant ProteinsSequence AlignmentSequence Homology, Amino AcidSequence Homology, Nucleic AcidTumor Suppressor Protein p53Hordeum vulgare subsp. vulgare
TNO Identifier
236660
ISSN
00145793
Source
FEBS Letters, 526(1-3), pp. 53-57.
Pages
53-57