Unique complex between bacterial azurin and tumor-suppressor protein p53
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...
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| Published in | Biochemical and biophysical research communications Vol. 332; no. 4; pp. 965 - 968 |
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| Main Authors | , |
| Format | Journal Article |
| Language | English |
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Elsevier Inc
15.07.2005
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| Abstract | 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 time, here we demonstrate and characterize this proposed complex using purified proteins in vitro. We find that azurin binds to p53 with nanomolar affinity in a four-to-one stoichiometry (pH 7.5, 25
°C). Upon azurin binding, secondary structure is induced and tryptophan fluorescence is quenched, implying that interactions occur in the N-terminal p53 domain which is also the binding site for many oncogenes. Further biophysical studies may assist the design of novel cancer treatments that are based on azurin. |
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| AbstractList | 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 time, here we demonstrate and characterize this proposed complex using purified proteins in vitro. We find that azurin binds to p53 with nanomolar affinity in a four-to-one stoichiometry (pH 7.5, 25 degrees C). Upon azurin binding, secondary structure is induced and tryptophan fluorescence is quenched, implying that interactions occur in the N-terminal p53 domain which is also the binding site for many oncogenes. Further biophysical studies may assist the design of novel cancer treatments that are based on azurin. 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 time, here we demonstrate and characterize this proposed complex using purified proteins in vitro. We find that azurin binds to p53 with nanomolar affinity in a four-to-one stoichiometry (pH 7.5, 25 super(o)C). Upon azurin binding, secondary structure is induced and tryptophan fluorescence is quenched, implying that interactions occur in the N-terminal p53 domain which is also the binding site for many oncogenes. Further biophysical studies may assist the design of novel cancer treatments that are based on azurin. 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 time, here we demonstrate and characterize this proposed complex using purified proteins in vitro. We find that azurin binds to p53 with nanomolar affinity in a four-to-one stoichiometry (pH 7.5, 25 °C). Upon azurin binding, secondary structure is induced and tryptophan fluorescence is quenched, implying that interactions occur in the N-terminal p53 domain which is also the binding site for many oncogenes. Further biophysical studies may assist the design of novel cancer treatments that are based on azurin. |
| Author | Apiyo, David Wittung-Stafshede, Pernilla |
| Author_xml | – sequence: 1 givenname: David surname: Apiyo fullname: Apiyo, David organization: Department of Biochemistry and Cell Biology, Rice University, 6100 Main Street, Houston, TX 77251, USA – sequence: 2 givenname: Pernilla surname: Wittung-Stafshede fullname: Wittung-Stafshede, Pernilla email: pernilla@rice.edu organization: Department of Biochemistry and Cell Biology, Rice University, 6100 Main Street, Houston, TX 77251, USA |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/15913547$$D View this record in MEDLINE/PubMed |
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| Keywords | Azurin Protein–protein interactions Tumor-suppressor protein p53 Isothermal titration calorimetry Blue-copper protein Circular dichroism |
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| Snippet | The tumor-suppressor protein p53 is a major player in regulation of cell growth, genomic stability, and cell death. Recent work suggests that
Pseudomonas... The tumor-suppressor protein p53 is a major player in regulation of cell growth, genomic stability, and cell death. Recent work suggests that Pseudomonas... |
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| SubjectTerms | 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 |
| Title | Unique complex between bacterial azurin and tumor-suppressor protein p53 |
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