Establishment of Centromeric Chromatin by the CENP-A Assembly Factor CAL1 Requires FACT-Mediated Transcription

Chen, Chin-Chi; Bowers, Sarion R.; Lipinszki, Zoltán; Palladino, Jason; Trusiak, Sarah; Bettini, Emily; Rosin, Leah F.; Przewloka, Marcin R.; Glover, David M.; O’Neill, Rachel J.; Mellone, Barbara G.

doi:10.1016/j.devcel.2015.05.012

Cited by 118 publications

(126 citation statements)

References 63 publications

(96 reference statements)

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“…We also found that the chromatin-remodeling complex FACT, including Pof3 and Spt16, interacts with CENP-A cnp1 (Figure 3C). Consistent with these findings, CENP-A has been shown to be associated with the FACT complex in Drosophila and human cells (Boltengagen et al, 2015; Chen et al, 2015; Foltz et al, 2006; Okada et al, 2009). In addition, a conserved centromere protein, CENP-T (Cnp20 in fission yeast) copurified with CENP-A cnp1 .…”

Section: Resultssupporting

confidence: 65%

Ccp1 Homodimer Mediates Chromatin Integrity by Antagonizing CENP-A Loading

et al. 2016

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SUMMARY CENP-A is a centromere-specific histone 3 variant essential for centromere specification. CENP-A partially replaces canonical histone H3 at the centromeres. How the particular CENP-A/H3 ratio at centromeres is precisely maintained is unknown. It also remains unclear how CENP-A is excluded from non-centromeric chromatin. Here we identify Ccp1, an uncharacterized NAP family protein in fission yeast that antagonizes CENP-A loading at both centromeric and non-centromeric regions. Like the CENP-A loading factor HJURP, Ccp1 interacts with CENP-A, and is recruited to centromeres at the end of mitosis in a Mis16-dependent manner. These data indicate that factors with opposing CENP-A loading activities are recruited to centromeres. Furthermore, Ccp1 also cooperates with H2A.Z to evict CENP-A assembled in euchromatin. Structural analyses indicate that Ccp1 forms a homodimer that is required for its anti-CENP-A loading activity. Our study establishes mechanisms for maintenance of CENP-A homeostasis at centromeres and the prevention of ectopic assembly of centromeres.

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Section: Resultssupporting

confidence: 65%

Ccp1 Homodimer Mediates Chromatin Integrity by Antagonizing CENP-A Loading

et al. 2016

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“…In addition, activation or repression of transcription from a Human Artificial Chromosomes (HAC) alters the stability of the HAC (Nakano et al, 2008). Recent work in Drosophila demonstrated that the act of transcription, rather than the resulting RNA, is required for normal Cenp-A deposition (Chen et al, 2015). While several other studies have depleted centromeric RNAs and concluded that cen-RNA is required for various mitotic processes (Ideue et al, 2014; Liu et al, 2015; Quenet and Dalal, 2014; Rosic et al, 2014).…”

Section: Discussionmentioning

confidence: 99%

Centromeric Transcription Regulates Aurora-B Localization and Activation

Blower

2016

Cell Reports

105

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Summary Centromeric transcription is widely conserved, however it is not clear what role centromere transcription plays during mitosis. Here I find that centromeres are transcribed in Xenopus egg extracts into a long noncoding RNA (lncRNA; cen-RNA) that localizes to mitotic centromeres, chromatin, and spindles. Cen-RNAs bind to the Chromosomal Passenger Complex (CPC) in vitro and in vivo. Blocking transcription or antisense inhibition of cen-RNA leads to a reduction of CPC localization to the inner centromere and misregulation of CPC component Aurora-B activation, independently of known centromere recruitment pathways. Additionally, transcription is required for normal bipolar attachment of kinetochores to the mitotic spindle, consistent with a role for cen-RNA in CPC regulation. This work demonstrates that cen-RNAs promote normal kinetochore function through regulation of the localization and activation of the CPC and confirm that lncRNAs are components of the centromere.

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“…For example, CAL1 also interacts with the highly conserved FACT complex (Chen et al, 2015) and localizes to the nucleolus (Chen et al, 2012; Lidsky et al, 2013). We hypothesize that the overall CAL1 sequence is under purifying selection (Phansalkar et al, 2012) to preserve its functional interactions with highly conserved partners, while key residues within the N terminus of CAL1 evolve to maintain the functional interaction with CENP-A.…”

Section: Discussionmentioning

confidence: 99%

Co-evolving CENP-A and CAL1 Domains Mediate Centromeric CENP-A Deposition across Drosophila Species

Rosin

Mellone

2016

Developmental Cell

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SUMMARY Centromeres mediate the conserved process of chromosome segregation, yet centromeric DNA and the centromeric histone, CENP-A, are rapidly evolving. The rapid evolution of Drosophila CENP-A loop 1 (L1) is thought to modulate the DNA-binding preferences of CENP-A to counteract centromere drive, the preferential transmission of chromosomes with expanded centromeric satellites. Consistent with this model, CENP-A from Drosophila bipectinata (bip) cannot localize to Drosophila melanogaster (mel) centromeres. We show that this result is due to the inability of the mel CENP-A chaperone, CAL1, to deposit bip CENP-A into chromatin. Co-expression of bip CENP-A and bip CAL1 in mel cells restores centromeric localization, and similar findings apply to other Drosophila species. We identify two co-evolving regions, CENP-A L1 and the CAL1 N terminus, as critical for lineage-specific CENP-A incorporation. Collectively, our data show that the rapid evolution of L1 modulates CAL1-mediated CENP-A assembly, suggesting an alternative mechanism for the suppression of centromere drive.

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Establishment of Centromeric Chromatin by the CENP-A Assembly Factor CAL1 Requires FACT-Mediated Transcription

Cited by 118 publications

References 63 publications

Ccp1 Homodimer Mediates Chromatin Integrity by Antagonizing CENP-A Loading

Ccp1 Homodimer Mediates Chromatin Integrity by Antagonizing CENP-A Loading

Centromeric Transcription Regulates Aurora-B Localization and Activation

Co-evolving CENP-A and CAL1 Domains Mediate Centromeric CENP-A Deposition across Drosophila Species

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