Related Experiment Video
Updated: Sep 27, 2026

Escherichia coli -Based Complementation Assay to Study the Chaperone Function of Heat Shock Protein 70
Published on: March 8, 2024
Specific stimulation of human apurinic/apyrimidinic endonuclease by heat shock protein 70
Frances Mendez1, Margarita Sandigursky, Raichal P Kureekattil
1Department of Radiation Oncology, Montefiore Medical Center, Albert Einstein College of Medicine, 111 East 210 Street, Bronx, NY 10467, USA.
Abstract:
We previously demonstrated the stimulation of human apurinic/apyrimidinic endonuclease 1 (HAP1) by heat shock protein 70 (HSP70). In this work, we further defined the functional interaction between these proteins. Digestion of HSP70 by trypsin released 48 and 43 kDa amino terminal fragments that retained the ability to stimulate HAP1. In agreement with this result, an HSP70 N-terminal deletion mutant protein containing amino acids 1-385 was comparable to the full-length protein in its ability to enhance HAP1 activity. HSP70 mutants containing carboxy terminal amino acids 386-640 stimulated HAP1 only slightly, as did unrelated proteins. These results implicate the amino terminal portion of HSP70 in stimulating the activity of HAP1.
Related Concept Videos
Bacterial Protein Maturation
Molecular Chaperones and Protein Folding
The...
Regulation of the Unfolded Protein Response
Long-patch Base Excision Repair
Single-Strand DNA Binding Proteins

