A multi-layered structure of the interphase chromocenter revealed by proximity-based biotinylation.
Nucleic Acids Res
; 48(8): 4161-4178, 2020 05 07.
Article
in En
| MEDLINE
| ID: mdl-32182352
ABSTRACT
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.
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Chromosomal Proteins, Non-Histone
/
Centromere
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Drosophila Proteins
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Centromere Protein A
/
Interphase
Limits:
Animals
Language:
En
Journal:
Nucleic Acids Res
Year:
2020
Document type:
Article
Affiliation country:
Germany