Nitric oxide (NO) disrupts specific DNA binding of the transcription factor c-Myb in vitro

被引：43

作者：

Brendeford, EM ^{[1
]}

Andersson, KB ^{[1
]}

Gabrielsen, OS ^{[1
]}

机构：

[1] Univ Oslo, Dept Biochem, N-0316 Oslo 3, Norway

来源：

FEBS LETTERS | 1998年 / 425卷 / 01期

关键词：

Myb; DNA binding; avian myeloblastosis virus; nitric oxide; redox;

D O I：

10.1016/S0014-5793(98)00196-3

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：

In an attempt to elucidate signal transduction pathways which mag modulate DNA binding of the transcription factor c-Myb, we investigated whether c-Myb could be a target for the signaling molecule nitric oxide (NO) in vitro, NO-generating agents severely inhibited specific DNA binding of the c-Myb minimal DNA-binding domain R2R3., This inhibition was readily reversible upon treatment with excess DTT. A redox-sensitive cysteine (C130) was required for this NO sensitivity. Moreover, a DNA-binding domain carrying two of the avian myeloblastosis virus (AMV)-specific mutations (L106H, V117D) appeared to be less sensitive to S-nitrosylation than the wild-type c-Myb. This difference in NO sensitivity may influence the regulation of wild type versus AMV v-Myb protein function. (C) 1998 Federation of European Biochemical Societies.

引用

页码：52 / 56

页数：5

共 33 条

[11] SECONDARY STRUCTURE OF THE DNA-BINDING DOMAIN OF THE C-MYB ONCOPROTEIN IN SOLUTION - A MULTIDIMENSIONAL DOUBLE AND TRIPLE HETERONUCLEAR NMR-STUDY [J].