Apoptin protein multimers form distinct higher-order nucleoprotein complexes with DNA
JournalArticle (Originalarbeit in einer wissenschaftlichen Zeitschrift)
 
ID 4531057
Author(s) Leliveld, SR; Dame, RT; Mommaas, MA; Koerten, HK; Wyman, C; Danen-van Oorschot, AAAM; Rohn, JL; Noteborn, MHM; Abrahams, JP
Author(s) at UniBasel Abrahams, Jan Pieter
Year 2003
Title Apoptin protein multimers form distinct higher-order nucleoprotein complexes with DNA
Journal NUCLEIC ACIDS RESEARCH
Volume 31
Number 16
Pages / Article-Number 4805-4813
Mesh terms Science & TechnologyLife Sciences & BiomedicineBiochemistry & Molecular BiologyBiochemistry & Molecular Biology
Abstract

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.

Publisher OXFORD UNIV PRESS
ISSN/ISBN 0305-1048
Full Text on edoc
Digital Object Identifier DOI 10.1093/nar/gkg661; 10.1093/nar/gkg661
ISI-Number WOS:000184783000017
Document type (ISI) Article
   

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