ArticleProtein science : a publication of the Protein Society1999
In vitro evolution of thermostable p53 variants.
Article in Protein science : a publication of the Protein Society, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Stabilization of G protein-coupled receptors by point mutations.Frontiers in pharmacology · 2015Review
- Thermostability of in vitro evolved Bacillus subtilis lipase A: a network and dynamics perspective.PloS one · 2014Article
- Stability of p53 homologs.PloS one · 2012Article
- Stabilising the DNA-binding domain of p53 by rational design of its hydrophobic core.Protein engineering, design & selection : PEDS · 2009Article
- Stability of the core domain of p53: insights from computer simulations.BMC bioinformatics · 2008Article
- Review
- Folding and misfolding mechanisms of the p53 DNA binding domain at physiological temperature.Protein science : a publication of the Protein Society · 2006Article
- Rational design of p53, an intrinsically unstructured protein, for the fabrication of novel molecular sensors.The Journal of biological chemistry · 2005Article
- Laboratory-directed protein evolution.Microbiology and molecular biology reviews : MMBR · 2005Review
- eCodonOpt: a systematic computational framework for optimizing codon usage in directed evolution experiments.Nucleic acids research · 2002Article
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The tumor suppressor p53 is conformationally unstable at physiological temperature. Even the activated p53delta30 variant, which lacks the self-inhibiting carboxy terminal domain, has a half-life of only 8 min at 37 degrees C in vitro. We have developed a genetic approach to identify p53 variants that stabilize the active conformation. The human p53delta30 gene was randomly mutated, and the resulting library was expressed in Escherichia coli under conditions that apparently denatured the parental protein. Stable p53 variants were identified based on their ability to specifically bind a p53 consensus site. The initial thermostable variants were randomly recombined by DNA shuffling, and substitutions that were functionally additive or synergistic were identified in a second more stringent round of screening. The DNA binding activity of N239Y/N268D/E336V p53delta30 variant has a half-life of 100 min at 37 degrees C, 12 times longer than that of the parental protein. The thermostable variants should be more amenable to crystallographic studies and more effective in gene therapies than the wild-type protein.
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