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Nicotinamide adenine dinucleotide stimulates oligomerization, interaction with adenovirus E1A and an intrinsic dehydrogenase activity of CtBP
Author(s) -
Balasubramanian P.,
Zhao Ling-Jun,
Chinnadurai G.
Publication year - 2003
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(03)00119-4
Subject(s) - nad+ kinase , corepressor , nicotinamide adenine dinucleotide , chemistry , dehydrogenase , biochemistry , transcription (linguistics) , enzyme , transcriptional regulation , transcription factor , microbiology and biotechnology , biology , repressor , gene , linguistics , philosophy
The C‐terminal region of adenovirus E1A interacts with the transcriptional corepressor, CtBP. The mechanism of transcriptional regulation by CtBP is not known. CtBP shares a significant homology with NAD + ‐dependent D2‐hydroxy acid dehydrogenases. CtBP binds to NAD + and NADH. Both forms of the dinucleotide stimulate oligomerization of native CtBP and enhance complex formation with E1A. CtBP also has a slow dehydrogenase activity. Interaction of CtBP with E1A reduces the dehydrogenase activity. Our results raise the possibility that the oxidation/reduction reactions of CtBP may regulate transcription. Thus, CtBP is a unique transcriptional regulator with an enzymatic activity similar to metabolic dehydrogenases. The levels of intracellular nicotinamide adenine dinucleotide may modulate transcriptional activity of CtBP.