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Kochanova, N.Y.* ; Schauer, T.* ; Mathias, G.P.* ; Lukacs, A.* ; Schmidt, A.* ; Flatley, A. ; Schepers, A. ; Thomae, A.W.* ; Imhof, A.*

A multi-layered structure of the interphase chromocenter revealed by proximity-based biotinylation.

Nucleic Acids Res. 48, 4161-4178 (2020)
Publ. Version/Full Text Research data DOI
Open Access Gold
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During interphase centromeres often coalesce into a small number of chromocenters, which can be visualized as distinct, DAPI dense nuclear domains. Intact chromocenters play a major role in maintaining genome stability as they stabilize the transcriptionally silent state of repetitive DNA while ensuring centromere function. Despite its biological importance, relatively little is known about the molecular composition of the chromocenter or the processes that mediate chromocenter formation and maintenance. To provide a deeper molecular insight into the composition of the chromocenter and to demonstrate the usefulness of proximity-based biotinylation as a tool to investigate those questions, we performed super resolution microscopy and proximity-based biotinylation experiments of three distinct proteins associated with the chromocenter in Drosophila. Our work revealed an intricate internal architecture of the chromocenter suggesting a complex multilayered structure of this intranuclear domain.
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Publication type Article: Journal article
Document type Scientific Article
Keywords Drosophila-melanogaster; Heterochromatin Protein-1; Phase-separation; Satellite Dna; In-vivo; Chromatin; Mouse; Identification; Transcription; Localization
ISSN (print) / ISBN 0305-1048
e-ISSN 1362-4962
Quellenangaben Volume: 48, Issue: 8, Pages: 4161-4178 Article Number: , Supplement: ,
Publisher Oxford University Press
Publishing Place Great Clarendon St, Oxford Ox2 6dp, England
Reviewing status Peer reviewed
Institute(s) Monoclonal Antibody (IDO-MAB)
Grants DFG
Graduate School of Quantitative Biosciences Munich (QBM)
Deutsche Forschungsgemeinschaft (DFG)