Apurinic/apyrimidinic (AP) site recognition by the 5′-dRP/AP lyase in poly(ADP-ribose) polymerase-1 (PARP-1)

被引：125

作者：

Khodyreva, S. N. ^{[1
]}

Prasad, R. ^{[2
]}

Ilina, E. S. ^{[1
]}

Sukhanova, M. V. ^{[1
]}

Kutuzov, M. M. ^{[1
]}

Liu, Y. ^{[2
]}

Hou, E. W. ^{[2
]}

Wilson, S. H. ^{[2
]}

Lavrik, O. I. ^{[1
]}

机构：

[1] Russian Acad Sci, Inst Chem Biol & Fundamental Med, Siberian Branch, Novosibirsk, Russia

[2] NIEHS, NIH, Res Triangle Pk, NC 27709 USA

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 2010年 / 107卷 / 51期

基金：

俄罗斯基础研究基金会; 美国国家卫生研究院;

关键词：

Schiff base; apurinic/apyrimidinic site-binding protein; BASE-EXCISION-REPAIR; DNA-REPAIR; ABASIC SITES; MAMMALIAN-CELLS; BETA; ENDONUCLEASE; DAMAGE; PROTEINS; CLEAVAGE; ENZYMES;

D O I：

10.1073/pnas.1009182107

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

The capacity of human poly(ADP-ribose) polymerase-1 (PARP-1) to interact with intact apurinic/apyrimidinic (AP) sites in DNA has been demonstrated. In cell extracts, sodium borohydride reduction of the PARP-1/AP site DNA complex resulted in covalent cross-linking of PARP-1 to DNA; the identity of cross-linked PARP-1 was confirmed by mass spectrometry. Using purified human PARP-1, the specificity of PARP-1 binding to AP site-containing DNA was confirmed in competition binding experiments. PARP-1 was only weakly activated to conduct poly(ADP-ribose) synthesis upon binding to AP site-containing DNA, but was strongly activated for poly (ADP-ribose) synthesis upon strand incision by AP endonuclease 1 (APE1). By virtue of its binding to AP sites, PARP-1 could be poised for its role in base excision repair, pending DNA strand incision by APE1 or the 5'-dRP/AP lyase activity in PARP-1.

引用

页码：22090 / 22095

页数：6

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