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

被引：73

作者：

Balasubramanian, P ^{[1
]}

Zhao, LJ ^{[1
]}

Chinnadurai, G ^{[1
]}

机构：

[1] St Louis Univ, Ctr Hlth Sci, Inst Mol Virol, St Louis, MO 63110 USA

来源：

FEBS LETTERS | 2003年 / 537卷 / 1-3期

关键词：

CtBP; corepressor; E1A; NAD(+)/NADH; dehydrogenase;

D O I：

10.1016/S0014-5793(03)00119-4

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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. (C) 2003 Published by Elsevier Science B.V. on behalf of the Federation of European Biochemical Societies.

引用

页码：157 / 160

页数：4

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