Nicotinamide adenine dinucleotide stimulates oligomerization, interaction with adenovirus E1A and an intrinsic dehydrogenase activity of CtBP

FEBS Lett. 2003 Feb 27;537(1-3):157-60. doi: 10.1016/s0014-5793(03)00119-4.

Abstract

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.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Adenovirus E1A Proteins / chemistry
  • Adenovirus E1A Proteins / metabolism*
  • Alcohol Oxidoreductases
  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • Cloning, Molecular
  • DNA-Binding Proteins / chemistry
  • DNA-Binding Proteins / metabolism*
  • Escherichia coli / genetics
  • Kinetics
  • Macromolecular Substances
  • NAD / pharmacology*
  • Oxidation-Reduction
  • Oxidoreductases / chemistry
  • Oxidoreductases / metabolism*
  • Phosphoproteins / chemistry
  • Phosphoproteins / metabolism*
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / metabolism
  • Vertebrates

Substances

  • Adenovirus E1A Proteins
  • DNA-Binding Proteins
  • Macromolecular Substances
  • Phosphoproteins
  • Recombinant Proteins
  • NAD
  • Oxidoreductases
  • Alcohol Oxidoreductases
  • C-terminal binding protein