A tormentor in the quest for plant p53-like proteins.
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.
Center for Phytotechnology TNO/UL, Wassenaarseweg 64, 2333 AL Leiden, The Netherlands. korthout@voeding.tno.nl
Henrie A A J
HA
Korthout
Martien P M
MP
Caspers
Marijke J
MJ
Kottenhagen
Quinta
Q
Helmer
Mei
M
Wang
D000595:Amino Acid Sequence; D001483:Base Sequence; D001467:Hordeum / Q000201:enzymology / Q000502:physiology*; D007655:Ketoglutarate Dehydrogenase Complex / Q000737:chemistry*; D008969:Molecular Sequence Data; D010940:Plant Proteins / Q000737:chemistry*; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D012689:Sequence Homology, Nucleic Acid; D016159:Tumor Suppressor Protein p53 / Q000737:chemistry* / Q000378:metabolism
D010940:Plant Proteins; D016159:Tumor Suppressor Protein p53; D007655:Ketoglutarate Dehydrogenase Complex