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A tormentor in the quest for plant p53‐like proteins
Author(s) -
Korthout Henrie A.A.J,
Caspers Martien P.M,
Kottenhagen Marijke J,
Helmer Quinta,
Wang Mei
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(02)03113-7
Subject(s) - complementary dna , epitope , microbiology and biotechnology , biology , biochemistry , cdna library , monoclonal antibody , dehydrogenase , peptide sequence , protein sequencing , antibody , genetics , enzyme , gene
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.