Interaction of Oct-1 and automodification domain of poly(ADP-ribose) synthetase

被引：80

作者：

Nie, J ^{[1
]}

Sakamoto, S ^{[1
]}

Song, DM ^{[1
]}

Qu, ZQ ^{[1
]}

Ota, K ^{[1
]}

Taniguchi, T ^{[1
]}

机构：

[1] Kochi Med Sch, Med Res Ctr, Mol Biol Lab, Nanko Ku, Kochi 7838505, Japan

来源：

FEBS LETTERS | 1998年 / 424卷 / 1-2期

关键词：

poly(ADP-ribose) synthetase; Oct-1; two-hybrid system;

D O I：

10.1016/S0014-5793(98)00131-8

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：

We isolated several clones from a matchmaker two-hybrid system human lymphocyte cDNA library using an automodification domain of poly(ADP-ribose) synthetase (PARS) as a probe. A DNA sequence (similar to 1 kbp) of the clone was identical to part of the Oct-1 DNA sequence. We then constructed either a His-tagged or GST fusion protein of the inserted cDNA from the clone and the fusion protein was shown to interact with PARS by far-Western blot analysis and coprecipitation with affinity resin. Furthermore, the His-tagged Oct-1/POU-homeo fusion protein interacted weakly with the octamer motif of the DRa promoter and the addition of PARS fusion protein greatly increased the DNA binding activity. These results suggest that PARS interacts with Oct-1 and stabilizes the binding of Oct-1 to the octamer motif. (C) 1998 Federation of European Biochemical Societies.

引用

页码：27 / 32

页数：6

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