Stability of p53 homologs
Most proteins have not evolved for maximal thermal stability. Some are only marginally stable, as for example, the DNA-binding domains of p53 and its homologs, whose kinetic and thermodynamic stabilities are strongly correlated. Here, we applied high-throughput methods using a real-time PCR thermocy...
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| Veröffentlicht in: | PloS one 2012-10, Vol.7 (10), p.e47889 |
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| description | Most proteins have not evolved for maximal thermal stability. Some are only marginally stable, as for example, the DNA-binding domains of p53 and its homologs, whose kinetic and thermodynamic stabilities are strongly correlated. Here, we applied high-throughput methods using a real-time PCR thermocycler to study the stability of several full-length orthologs and paralogs of the p53 family of transcription factors, which have diverse functions, ranging from tumour suppression to control of developmental processes. From isothermal denaturation fluorimetry and differential scanning fluorimetry, we found that full-length proteins showed the same correlation between kinetic and thermodynamic stability as their isolated DNA-binding domains. The stabilities of the full-length p53 orthologs were marginal and correlated with the temperature of their organism, paralleling the stability of the isolated DNA-binding domains. Additionally, the paralogs p63 and p73 were significantly more stable and long-lived than p53. The short half-life of p53 orthologs and the greater persistence of the paralogs may be biologically relevant. |
| doi_str_mv | 10.1371/journal.pone.0047889 |
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Dafydd</contributor><creatorcontrib>Brandt, Tobias ; Kaar, Joel L ; Fersht, Alan R ; Veprintsev, Dmitry B ; Jones, D. Dafydd</creatorcontrib><description>Most proteins have not evolved for maximal thermal stability. Some are only marginally stable, as for example, the DNA-binding domains of p53 and its homologs, whose kinetic and thermodynamic stabilities are strongly correlated. Here, we applied high-throughput methods using a real-time PCR thermocycler to study the stability of several full-length orthologs and paralogs of the p53 family of transcription factors, which have diverse functions, ranging from tumour suppression to control of developmental processes. From isothermal denaturation fluorimetry and differential scanning fluorimetry, we found that full-length proteins showed the same correlation between kinetic and thermodynamic stability as their isolated DNA-binding domains. The stabilities of the full-length p53 orthologs were marginal and correlated with the temperature of their organism, paralleling the stability of the isolated DNA-binding domains. Additionally, the paralogs p63 and p73 were significantly more stable and long-lived than p53. The short half-life of p53 orthologs and the greater persistence of the paralogs may be biologically relevant.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0047889</identifier><identifier>PMID: 23112865</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Animals ; Anticoagulants ; Binding ; Binding Sites ; Biochemistry ; Biology ; Body temperature ; Correlation ; Dehydrogenases ; Denaturation ; Deoxyribonucleic acid ; DNA ; DNA binding proteins ; DNA-Binding Proteins - chemistry ; Drosophila ; Engineering ; Fluorimetry ; Homology ; Humans ; Insects ; Kinetics ; Laboratories ; Mice ; Molecular biology ; Mutation ; Nuclear Proteins - chemistry ; p53 Protein ; Protein Denaturation ; Protein Stability ; Protein Structure, Tertiary ; Proteins ; Studies ; Thermal stability ; Thermodynamics ; Transcription factors ; Transcription Factors - chemistry ; Tumor Protein p73 ; Tumor proteins ; Tumor Suppressor Protein p53 - chemistry ; Tumor Suppressor Proteins - chemistry ; Tumors ; Xenopus ; Xenopus laevis ; Zebrafish</subject><ispartof>PloS one, 2012-10, Vol.7 (10), p.e47889</ispartof><rights>COPYRIGHT 2012 Public Library of Science</rights><rights>2012. This is an open-access article, free of all copyright, and may be freely reproduced, distributed, transmitted, modified, built upon, or otherwise used by anyone for any lawful purpose. The work is made available under the Creative Commons CC0 public domain dedication. 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From isothermal denaturation fluorimetry and differential scanning fluorimetry, we found that full-length proteins showed the same correlation between kinetic and thermodynamic stability as their isolated DNA-binding domains. The stabilities of the full-length p53 orthologs were marginal and correlated with the temperature of their organism, paralleling the stability of the isolated DNA-binding domains. Additionally, the paralogs p63 and p73 were significantly more stable and long-lived than p53. The short half-life of p53 orthologs and the greater persistence of the paralogs may be biologically relevant.</description><subject>Animals</subject><subject>Anticoagulants</subject><subject>Binding</subject><subject>Binding Sites</subject><subject>Biochemistry</subject><subject>Biology</subject><subject>Body temperature</subject><subject>Correlation</subject><subject>Dehydrogenases</subject><subject>Denaturation</subject><subject>Deoxyribonucleic acid</subject><subject>DNA</subject><subject>DNA binding proteins</subject><subject>DNA-Binding Proteins - chemistry</subject><subject>Drosophila</subject><subject>Engineering</subject><subject>Fluorimetry</subject><subject>Homology</subject><subject>Humans</subject><subject>Insects</subject><subject>Kinetics</subject><subject>Laboratories</subject><subject>Mice</subject><subject>Molecular biology</subject><subject>Mutation</subject><subject>Nuclear Proteins - chemistry</subject><subject>p53 Protein</subject><subject>Protein Denaturation</subject><subject>Protein Stability</subject><subject>Protein Structure, Tertiary</subject><subject>Proteins</subject><subject>Studies</subject><subject>Thermal stability</subject><subject>Thermodynamics</subject><subject>Transcription factors</subject><subject>Transcription Factors - 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| subjects | Animals Anticoagulants Binding Binding Sites Biochemistry Biology Body temperature Correlation Dehydrogenases Denaturation Deoxyribonucleic acid DNA DNA binding proteins DNA-Binding Proteins - chemistry Drosophila Engineering Fluorimetry Homology Humans Insects Kinetics Laboratories Mice Molecular biology Mutation Nuclear Proteins - chemistry p53 Protein Protein Denaturation Protein Stability Protein Structure, Tertiary Proteins Studies Thermal stability Thermodynamics Transcription factors Transcription Factors - chemistry Tumor Protein p73 Tumor proteins Tumor Suppressor Protein p53 - chemistry Tumor Suppressor Proteins - chemistry Tumors Xenopus Xenopus laevis Zebrafish |
| title | Stability of p53 homologs |
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