Abstract
The alpha splice variant of p73 (p73alpha), a homologue of the tumor suppressor p53, has close to its C terminus a sterile alpha motif (SAM), SAMp73, that is thought to be involved in protein-protein interactions. Here, we report the lipid binding properties of this domain. Binding was assayed against zwitterionic (phosphatidylcholine) and anionic (phosphatidic acid) lipids and was studied by different biophysical techniques, namely, circular dichroism and fluorescence spectroscopies and differential scanning calorimetry. These techniques unambiguously indicate that SAMp73 binds to lipids. The binding involves protein surface attachment and partial membrane penetration, accompanied by changes in SAMp73 structure.
Highlights
P73 and p63 are members of the p53 gene family [1, 2]
Binding of SAMp73 to Lipid Membranes—SAM domains were first described as a module present in a small group of yeast sexual differentiation and Drosophila polyhomeotic proteins [43]
These domains were subsequently found in other proteins involved in the regulation of numerous developmental processes among eukaryotes, suggesting that SAM domains were evolutionarily conserved
Summary
Trizma base, and NaCl were from Sigma. ⌻he Ni2ϩnitrilotriacetic acid resin was from Invitrogen.
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