Apoptin's functional N- and C-termini independently bind DNA
JournalArticle (Originalarbeit in einer wissenschaftlichen Zeitschrift)
ID 4531041
Author(s) Leliveld, SR; Dame, RT; Rohn, JL; Noteborn, MHM; Abrahams, JP
Author(s) at UniBasel Abrahams, Jan Pieter
Year 2004
Title Apoptin's functional N- and C-termini independently bind DNA
Volume 557
Number 1-3
Pages / Article-Number 155-158
Keywords Apoptin; apoptosis; DNA interaction; multimerisation; protein-DNA superstructure
Mesh terms Science & TechnologyLife Sciences & BiomedicineBiochemistry & Molecular BiologyBiophysicsCell BiologyBiochemistry & Molecular BiologyBiophysicsCell Biology

Apoptin induces apoptosis specifically in tumour cells, where Apoptin is enriched in the DNA-dense heterochromatin and nucleoli. In vitro, Apoptin interacts with dsDNA, forming large nucleoprotein superstructures likely to be relevant for apoptosis induction. Its N- and C-terminal domains also have cell-killing activity, although they are less potent than the full-length protein. Here, we report that both Apoptin's Nand C-terminal halves separately bound DNA, indicating multiple independent binding sites. The reduced cell killing activity of both truncation mutants was mirrored in vitro by a reduced affinity compared to full-length Apoptin. However, none of the truncation mutants cooperatively bound DNA or formed superstructures, which suggests that cooperative DNA binding by Apoptin is required for the formation of nucleoprotein superstructures. As Apoptin's N- and C-terminal fragments not only share apoptotic activity, but also affinity for DNA, we propose that both properties are functionally linked. (C) 2003 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

ISSN/ISBN 0014-5793
Full Text on edoc
Digital Object Identifier DOI 10.1016/S0014-5793(03)01465-0; 10.1016/S0014-5793(03)01465-0
ISI-Number WOS:000188648100028
Document type (ISI) Article

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