Apoptin protein multimers form distinct higher-order nucleoprotein complexes with DNA

Leliveld, Sirik R. and Dame, Remus T. and Mommaas, Mieke A. and Koerten, Henk K. and Wyman, Claire and Danen-van Oorschot, Astrid A. A. M. and Rohn, Jennifer L. and Noteborn, Mathieu H. M. and Abrahams, Jan Pieter. (2003) Apoptin protein multimers form distinct higher-order nucleoprotein complexes with DNA. Nucleic Acids Research, 31 (16). pp. 4805-4813.

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Official URL: https://edoc.unibas.ch/75973/

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The chicken anaemia virus-derived protein apoptin is a tumour-specific cell-killing agent. It is biologically active as a highly stable, multimeric complex, consisting of 30-40 monomers. In tumour cells, but negligibly in normal cells, apoptin is imported into the nucleus prior to the induction of apoptosis. Immunoelectron microscopic data we report here indicate that apoptin predominantly co-localises with heterochromatin and nucleoli within tumour cells. Apoptin's preference for these DNA-dense nuclear bodies may be explained by our finding that apoptin cooperatively forms distinct superstructures with DNA in vitro. These superstructures do not grow beyond a diameter of similar to200 nm, containing up to 20 multimeric apoptin complexes and similar to3 kb of DNA. Furthermore, we show a single apoptin multimer to have eight independent, non-specific DNA-binding sites which preferentially bind strand ends, but which can also collaborate to bind longer stretches of DNA. Apoptin's high affinity for naked, undecorated double- and single-stranded DNA and for DNA fibre ends suggests that it may also capture such DNA in superstructures in vivo. Since these forms of DNA are predominantly found in transcriptionally active, replicating and damaged DNA, apoptin could be triggering apoptosis by interfering with DNA transcription and synthesis.
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
Publisher:Oxford University Press
Note:Publication type according to Uni Basel Research Database: Journal article
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Last Modified:05 Nov 2020 15:48
Deposited On:05 Nov 2020 15:48

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