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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| Veröffentlicht in: | Biochemical and biophysical research communications 2005-07, Vol.332 (4), p.965-968 |
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| creator | Apiyo, David Wittung-Stafshede, Pernilla |
| description | 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. |
| doi_str_mv | 10.1016/j.bbrc.2005.05.038 |
| format | Article |
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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
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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.</description><subject>Azurin</subject><subject>Azurin - chemistry</subject><subject>Bacteria</subject><subject>Binding Sites</subject><subject>Biophysics - methods</subject><subject>Blue-copper protein</subject><subject>Calorimetry</subject><subject>Chromatography, Gel</subject><subject>Circular Dichroism</subject><subject>Humans</subject><subject>Isothermal titration calorimetry</subject><subject>Kinetics</subject><subject>Oxidation-Reduction</subject><subject>Protein Binding</subject><subject>Protein Folding</subject><subject>Protein Structure, Secondary</subject><subject>Protein Structure, Tertiary</subject><subject>Protein–protein interactions</subject><subject>Pseudomonas aeruginosa</subject><subject>Pseudomonas aeruginosa - metabolism</subject><subject>Temperature</subject><subject>Thermodynamics</subject><subject>Tryptophan - chemistry</subject><subject>Tumor Suppressor Protein p53 - chemistry</subject><subject>Tumor-suppressor protein p53</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkU1LxEAMhgdRdF39Ax6kJ29dk5lO2wEvIuoKghcFb8N0msIs_XKm9evX27IL3pQEcsiTNyEvY2cIKwRMLzerovB2xQHkak6R77EFgoKYIyT7bAEAacwVvh6x4xA2AIhJqg7ZEUqFQibZgq1fWvc2UmS7pq_pMypo-CBqo8LYgbwzdWS-R-_ayLRlNIxN5-Mw9r2nEDof9b4baGr2Upywg8rUgU53dcle7m6fb9bx49P9w831Y2wTTIeYp5IjWsgRrEIui5wEzxXnmRIVyATQ5BVl3GQWK5MDwtQXZV6kaSENZmLJLra60-7p8DDoxgVLdW1a6sag00xxkAj_gqiUwkTJ_8FMglBTLBnfgtZ3IXiqdO9dY_yXRtCzI3qjZ0f07IieU-TT0PlOfSwaKn9HdhZMwNUWoOlr7468DtZRa6l0nuygy879pf8DFH2a3w</recordid><startdate>20050715</startdate><enddate>20050715</enddate><creator>Apiyo, David</creator><creator>Wittung-Stafshede, Pernilla</creator><general>Elsevier Inc</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>C1K</scope><scope>7T7</scope><scope>7TO</scope><scope>8FD</scope><scope>FR3</scope><scope>H94</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>20050715</creationdate><title>Unique complex between bacterial azurin and tumor-suppressor protein p53</title><author>Apiyo, David ; Wittung-Stafshede, Pernilla</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c416t-265211c0810c9125b8e328922793f05401a8fe72a7c1fa8010e323d8b66b5a173</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2005</creationdate><topic>Azurin</topic><topic>Azurin - chemistry</topic><topic>Bacteria</topic><topic>Binding Sites</topic><topic>Biophysics - methods</topic><topic>Blue-copper protein</topic><topic>Calorimetry</topic><topic>Chromatography, Gel</topic><topic>Circular Dichroism</topic><topic>Humans</topic><topic>Isothermal titration calorimetry</topic><topic>Kinetics</topic><topic>Oxidation-Reduction</topic><topic>Protein Binding</topic><topic>Protein Folding</topic><topic>Protein Structure, Secondary</topic><topic>Protein Structure, Tertiary</topic><topic>Protein–protein interactions</topic><topic>Pseudomonas aeruginosa</topic><topic>Pseudomonas aeruginosa - metabolism</topic><topic>Temperature</topic><topic>Thermodynamics</topic><topic>Tryptophan - chemistry</topic><topic>Tumor Suppressor Protein p53 - chemistry</topic><topic>Tumor-suppressor protein p53</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Apiyo, David</creatorcontrib><creatorcontrib>Wittung-Stafshede, Pernilla</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Apiyo, David</au><au>Wittung-Stafshede, Pernilla</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Unique complex between bacterial azurin and tumor-suppressor protein p53</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>2005-07-15</date><risdate>2005</risdate><volume>332</volume><issue>4</issue><spage>965</spage><epage>968</epage><pages>965-968</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><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.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>15913547</pmid><doi>10.1016/j.bbrc.2005.05.038</doi><tpages>4</tpages></addata></record> |
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| source | MEDLINE; Elsevier ScienceDirect Journals Complete |
| 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 |
| title | Unique complex between bacterial azurin and tumor-suppressor protein p53 |
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