Journal
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volume 521, Issue 3, Pages 681-686Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2019.10.130
Keywords
Evolution; Structure; Tetramerization; Tumor suppressor protein p53
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Funding
- Photo-excitonix Project at Hokkaido University
- Natural Sciences and Engineering Council of Canada [RGPIN-05253-2017]
- JSPS [18J11518]
- [19K22240]
- Grants-in-Aid for Scientific Research [18J11518] Funding Source: KAKEN
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The p53 protein plays a number of roles in protecting organisms from different genotoxic stresses and this includes DNA damage induced by acetaldehyde, a metabolite of alcohol. Since the common tree shrew ingests high levels of alcohol as part of its normal diet, this suggests that its p53 protein may possess unique properties. Using a combination of biophysical and modeling studies, we demonstrate that the tetramerization domain of the tree shrew p53 protein is considerably more stable than the corresponding domain from humans despite sharing almost 90% sequence identity. Based on modeling and mutagenesis studies, we determine that a glutamine to methionine substitution at position 354 plays a key role in this difference. Given the link between stability of the p53 tetramerization domain and its transcriptional activity, the results suggest that this enhanced stability could lead to important consequences at p53-regulated genes in the tree shrew. (C) 2019 Elsevier Inc. All rights reserved.
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