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	J. Biol. Chem. Mar (2001); 276(12):9532-6
Heat shock protein 70 binds to human apurinic/apyrimidinic endonuclease and stimulates endonuclease activity at abasic sites.
Kenny MK, Mendez F, Sandigursky M, Kureekattil RP, Goldman JD, Franklin WA, Bases R
Department of Radiation Oncology, Montefiore Medical Center, Albert Einstein College of Medicine, Bronx, New York 10467, USA.
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.
[PUBMED: 11133992]