AI Article Synopsis
- HSP70 interacts with HAP1 through coimmunoprecipitation, indicating a physical connection between the two proteins.
- The combination of HSP70 and HAP1 results in increased endonuclease activity, enhancing DNA repair at abasic sites by 10-100 times.
- This interaction occurs independently of ATP and suggests that heat shock proteins like HSP70 may play a significant role in base excision repair, helping to protect cells from oxidative stress.
Article Abstract
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.
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| http://dx.doi.org/10.1074/jbc.M009297200 | DOI Listing |
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