Heat shock protein 70 binds to human apurinic/apyrimidinic endonuclease and stimulates endonuclease activity at abasic sites.
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.
Mesh Terms:
Base Sequence, Binding Sites, Carbon-Oxygen Lyases, DNA Primers, DNA-(Apurinic or Apyrimidinic Site) Lyase, Deoxyribonuclease IV (Phage T4-Induced), Enzyme Activation, HSP70 Heat-Shock Proteins, Humans, Precipitin Tests, Protein Binding, Recombinant Proteins
Base Sequence, Binding Sites, Carbon-Oxygen Lyases, DNA Primers, DNA-(Apurinic or Apyrimidinic Site) Lyase, Deoxyribonuclease IV (Phage T4-Induced), Enzyme Activation, HSP70 Heat-Shock Proteins, Humans, Precipitin Tests, Protein Binding, Recombinant Proteins
J. Biol. Chem.
Date: Mar. 23, 2001
PubMed ID: 11133992
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