Heat shock protein 70 binds to human apurinic/apyrimidinic endonuclease and stimulates endonuclease activity at abasic sites
Heat shock protein 70 binds to human apurinic/apyrimidinic endonuclease and stimulates endonuclease activity at abasic sites
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DOI：
10.1074/jbc.m009297200
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发表时间：
2001-03-23
影响因子：
4.8
通讯作者：
Bases, R
中科院分区：
文献类型：
--
作者：
Kenny, MK;Mendez, F;Bases, R
通过免疫共沉淀证明了人热休克蛋白 70 (HSP70) 与人脱嘌呤/脱嘧啶核酸内切酶 (HAP1) 的相互作用。 HSP70 和 HAP1 的组合还导致含有脱嘌呤/脱嘧啶位点的 DNA 片段的电泳迁移率发生变化。 HSP70/HAP1 相互作用的功能结果是脱碱基位点核酸内切酶活性增强 10-100 倍。 HSP70 和 HAP1 之间的物理和功能相互作用不需要添加 ATP。 HSP70 与关键碱基切除修复酶的关联表明热休克蛋白在促进碱基切除修复中发挥作用。这些发现提供了 HSP70 保护细胞免受氧化应激的可能机制。
The interaction of human heat shock protein 70 (HSP70) with human apurinic/apyrimidinic endonuclease (HAP1) was demonstrated by coimmunoprecipitation. A combination of HSP70 and HAP1 also caused a shift in the electrophoretic mobility of a DNA fragment containing an apurinic/apyrimidinic site. The functional consequence of the HSP70/HAP1 interaction was a 10-100-fold enhancement of endonuclease activity at abasic sites. The physical and functional interaction between HSP70 and HAP1 did not require the addition of ATP. The association of HSP70 and a key base excision repair enzyme suggests a role for heat shock proteins in promoting base excision repair. These findings provide a possible mechanism by which HSP70 protects cells against oxidative stress.