Structural highlights
FunctionPublication Abstract from PubMedMost members of the p53 family of transcription factors form tetramers. Responsible for determining the oligomeric state is a short oligomerization domain consisting of one beta-strand and one alpha-helix. With the exception of human p53 all other family members investigated so far contain a second alpha-helix as part of their tetramerization domain. Here we have used nuclear magnetic resonance spectroscopy to characterize the oligomerization domains of the two p53-like proteins from the tunicate Ciona intestinalis, representing the closest living relative of vertebrates. Structure determination reveals for one of the two proteins a new type of packing of this second alpha-helix on the core domain that was not predicted based on the sequence, while the other protein does not form a second helix despite the presence of crucial residues that are conserved in all other family members that form a second helix. By mutational analysis, we identify a proline as well as large hydrophobic residues in the hinge region between both helices as the crucial determinant for the formation of a second helix. Structural investigations of the p53/p73 homologs from the tunicate species Ciona intestinalis reveal the sequence requirements for the formation of a tetramerization domain.,Heering J, Jonker HR, Lohr F, Schwalbe H, Dotsch V Protein Sci. 2016 Feb;25(2):410-22. doi: 10.1002/pro.2830. Epub 2015 Nov 25. PMID:26473758[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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