Unique complex between bacterial azurin and tumor-suppressor protein p53

• Published in: Biochemical and biophysical research communications Vol. 332; no. 4; pp. 965 - 968
• Main Authors: Apiyo, David, Wittung-Stafshede, Pernilla
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 15.07.2005
• Subjects: Azurin; Azurin - chemistry; Bacteria; Binding Sites; Biophysics - methods; Blue-copper protein; Calorimetry; Chromatography, Gel; Circular Dichroism; Humans; Isothermal titration calorimetry; Kinetics; Oxidation-Reduction; Protein Binding; Protein Folding; Protein Structure, Secondary; Protein Structure, Tertiary; Protein–protein interactions; Pseudomonas aeruginosa; Pseudomonas aeruginosa - metabolism; Temperature; Thermodynamics; Tryptophan - chemistry; Tumor Suppressor Protein p53 - chemistry; Tumor-suppressor protein p53; Azurin; Protein–protein interactions; Tumor-suppressor protein p53; Isothermal titration calorimetry; Blue-copper protein; Circular dichroism

The tumor-suppressor protein p53 is a major player in regulation of cell growth, genomic stability, and cell death. Recent work suggests that Pseudomonas aeruginosa azurin, as the only bacterial protein known to date, can enter cancer cells and interact with p53 promoting cell death. For the first t...