Localization of Drosophila CENP-A to non-centromeric sites depends on the NuRD complex.
Animals
Cells, Cultured
Centromere
/ metabolism
Centromere Protein A
/ metabolism
Chromatin Assembly and Disassembly
/ physiology
Drosophila Proteins
/ genetics
Drosophila melanogaster
Mi-2 Nucleosome Remodeling and Deacetylase Complex
/ metabolism
Protein Domains
Retinoblastoma-Binding Protein 4
/ genetics
Trans-Activators
/ metabolism
Journal
Nucleic acids research
ISSN: 1362-4962
Titre abrégé: Nucleic Acids Res
Pays: England
ID NLM: 0411011
Informations de publication
Date de publication:
16 12 2019
16 12 2019
Historique:
accepted:
24
10
2019
revised:
12
09
2019
received:
21
02
2019
pubmed:
13
11
2019
medline:
15
5
2020
entrez:
13
11
2019
Statut:
ppublish
Résumé
Centromere function requires the presence of the histone H3 variant CENP-A in most eukaryotes. The precise localization and protein amount of CENP-A are crucial for correct chromosome segregation, and misregulation can lead to aneuploidy. To characterize the loading of CENP-A to non-centromeric chromatin, we utilized different truncation- and localization-deficient CENP-A mutant constructs in Drosophila melanogaster cultured cells, and show that the N-terminus of Drosophila melanogaster CENP-A is required for nuclear localization and protein stability, and that CENP-A associated proteins, rather than CENP-A itself, determine its localization. Co-expression of mutant CENP-A with its loading factor CAL1 leads to exclusive centromere loading of CENP-A whereas co-expression with the histone-binding protein RbAp48 leads to exclusive non-centromeric CENP-A incorporation. Mass spectrometry analysis of non-centromeric CENP-A interacting partners identified the RbAp48-containing NuRD chromatin remodeling complex. Further analysis confirmed that NuRD is required for ectopic CENP-A incorporation, and RbAp48 and MTA1-like subunits of NuRD together with the N-terminal tail of CENP-A mediate the interaction. In summary, our data show that Drosophila CENP-A has no intrinsic specificity for centromeric chromatin and utilizes separate loading mechanisms for its incorporation into centromeric and ectopic sites. This suggests that the specific association and availability of CENP-A interacting factors are the major determinants of CENP-A loading specificity.
Identifiants
pubmed: 31713634
pii: 5622714
doi: 10.1093/nar/gkz962
pmc: PMC7145711
doi:
Substances chimiques
Caf1-55 protein, Drosophila
0
Centromere Protein A
0
Cid protein, Drosophila
0
Drosophila Proteins
0
Retinoblastoma-Binding Protein 4
0
Trans-Activators
0
Mi-2 Nucleosome Remodeling and Deacetylase Complex
EC 3.5.1.98
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
11589-11608Informations de copyright
© The Author(s) 2019. Published by Oxford University Press on behalf of Nucleic Acids Research.
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