Prevalent conformations and subunit exchange in the biologically active apoptin protein multimer

Leliveld, Sirik R. and Noteborn, Mathieu H. M. and Abrahams, Jan Pieter. (2003) Prevalent conformations and subunit exchange in the biologically active apoptin protein multimer. European Journal of Biochemistry, 270 (17). pp. 3619-3627.

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Official URL: https://edoc.unibas.ch/75969/

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Recombinant, bacterially expressed apoptin protein induces apoptosis in human tumour cell lines but not in normal cells, mimicking the behaviour of ectopically expressed apoptin. Recombinant apoptin is isolated exclusively as a highly stable multimeric complex of 30-40 monomers, with little, if any, alpha-helical and beta-sheet structure. Despite its apparent disorder, multimeric apoptin is biologically active. Here, we present evidence that most of the apoptin moieties within the complex may well share a similar conformation. Furthermore, the multimer has extensive and uniform hydrophobic patches and conformationally stable domains. Only a small fraction of apoptin subunits can exchange between multimers under physiologically relevant conditions. These results prompt a model in which the apoptin multimer has a highly stable core of nonexchangeable subunits to which exchangeable subunits are attached through hydrophobic interactions. In combination with previous findings, our results lead us to propose that the stable core of apoptin is the biologically relevant structure.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Structural Biology & Biophysics > Nano-diffraction of Biological Specimen (Abrahams)
UniBasel Contributors:Abrahams, Jan Pieter
Item Type:Article, refereed
Article Subtype:Research Article
Note:Publication type according to Uni Basel Research Database: Journal article
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Last Modified:05 Nov 2020 15:43
Deposited On:05 Nov 2020 15:43

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