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.
机构:
Univ Paris 06, Lab BioMol, UMR 7203, F-75005 Paris, France
CNRS, UMR 7203, Paris, France
Ecole Normale Super, Dept Chim, F-75005 Paris, FranceUniv Paris 06, Lab BioMol, UMR 7203, F-75005 Paris, France
Carlier, Ludovic
Haase, A. Sander
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Univ Paris 06, Lab BioMol, UMR 7203, F-75005 Paris, France
CNRS, UMR 7203, Paris, France
Ecole Normale Super, Dept Chim, F-75005 Paris, FranceUniv Paris 06, Lab BioMol, UMR 7203, F-75005 Paris, France
Haase, A. Sander
Zepeda, Monica Y. Burgos
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Inst Pasteur, Dept Microbiol, Unite Membranes Bacteriennes, F-75724 Paris 15, France
CNRS, URA 2172, Paris, FranceUniv Paris 06, Lab BioMol, UMR 7203, F-75005 Paris, France
Zepeda, Monica Y. Burgos
Dassa, Elie
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Inst Pasteur, Dept Microbiol, Unite Membranes Bacteriennes, F-75724 Paris 15, France
CNRS, URA 2172, Paris, FranceUniv Paris 06, Lab BioMol, UMR 7203, F-75005 Paris, France