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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)

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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

Corresponding Author

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

Journal Nucleic Acids Research

Quellenangaben Volume: 48, Issue: 8, Pages: 4161-4178

Publisher Oxford University Press

Publishing Place Great Clarendon St, Oxford Ox2 6dp, England

Non-patent literature Publications

Reviewing status Peer reviewed

Institute(s) CF Monoclonal Antibodies (CF-MAB)

Grants DFG
Graduate School of Quantitative Biosciences Munich (QBM)
Deutsche Forschungsgemeinschaft (DFG)