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Article ; Online: The zinc-finger protein Z4 cooperates with condensin II to regulate somatic chromosome pairing and 3D chromatin organization.

Puerto, Marta / Shukla, Mamta / Bujosa, Paula / Pérez-Roldán, Juan / Torràs-Llort, Mònica / Tamirisa, Srividya / Carbonell, Albert / Solé, Carme / Puspo, Joynob Akter / Cummings, Christopher T / de Nadal, Eulàlia / Posas, Francesc / Azorín, Fernando / Rowley, M Jordan

Nucleic acids research

2024

Abstract: Chromosome pairing constitutes an important level of genome organization, yet the mechanisms that regulate pairing in somatic cells and the impact on 3D chromatin organization are still poorly understood. Here, we address these questions in Drosophila, ... ...

Abstract	Chromosome pairing constitutes an important level of genome organization, yet the mechanisms that regulate pairing in somatic cells and the impact on 3D chromatin organization are still poorly understood. Here, we address these questions in Drosophila, an organism with robust somatic pairing. In Drosophila, pairing preferentially occurs at loci consisting of numerous architectural protein binding sites (APBSs), suggesting a role of architectural proteins (APs) in pairing regulation. Amongst these, the anti-pairing function of the condensin II subunit CAP-H2 is well established. However, the factors that regulate CAP-H2 localization and action at APBSs remain largely unknown. Here, we identify two factors that control CAP-H2 occupancy at APBSs and, therefore, regulate pairing. We show that Z4, interacts with CAP-H2 and is required for its localization at APBSs. We also show that hyperosmotic cellular stress induces fast and reversible unpairing in a Z4/CAP-H2 dependent manner. Moreover, by combining the opposite effects of Z4 depletion and osmostress, we show that pairing correlates with the strength of intrachromosomal 3D interactions, such as active (A) compartment interactions, intragenic gene-loops, and polycomb (Pc)-mediated chromatin loops. Altogether, our results reveal new players in CAP-H2-mediated pairing regulation and the intimate interplay between inter-chromosomal and intra-chromosomal 3D interactions.
Language	English
Publishing date	2024-03-23
Publishing country	England
Document type	Journal Article
ZDB-ID	186809-3
ISSN	1362-4962 ; 1362-4954 ; 0301-5610 ; 0305-1048
ISSN (online)	1362-4962 ; 1362-4954
ISSN	0301-5610 ; 0305-1048
DOI	10.1093/nar/gkae198
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Article ; Online: Linker histone H1 regulates homeostasis of heterochromatin-associated cRNAs.

Bujosa, Paula / Reina, Oscar / Caballé, Adrià / Casas-Lamesa, Anna / Torras-Llort, Mònica / Pérez-Roldán, Juan / Nacht, Ana Silvina / Vicent, Guillermo P / Bernués, Jordi / Azorín, Fernando

Cell reports

2024 Volume 43, Issue 5, Page(s) 114137

Abstract: Chromatin-associated RNAs (cRNAs) are a poorly characterized fraction of cellular RNAs that co-purify with chromatin. Their full complexity and the mechanisms regulating their packaging and chromatin association remain poorly understood. Here, we address ...

Abstract	Chromatin-associated RNAs (cRNAs) are a poorly characterized fraction of cellular RNAs that co-purify with chromatin. Their full complexity and the mechanisms regulating their packaging and chromatin association remain poorly understood. Here, we address these questions in Drosophila. We find that cRNAs constitute a heterogeneous group of RNA species that is abundant in heterochromatic transcripts. We show that heterochromatic cRNAs interact with the heterogeneous nuclear ribonucleoproteins (hnRNP) hrp36/hrp48 and that depletion of linker histone dH1 impairs this interaction. dH1 depletion induces the accumulation of RNA::DNA hybrids (R-loops) in heterochromatin and, as a consequence, increases retention of heterochromatic cRNAs. These effects correlate with increased RNA polymerase II (RNAPII) occupancy at heterochromatin. Notably, impairing cRNA assembly by depletion of hrp36/hrp48 mimics heterochromatic R-loop accumulation induced by dH1 depletion. We also show that dH1 depletion alters nucleosome organization, increasing accessibility of heterochromatin. Altogether, these perturbations facilitate annealing of cRNAs to the DNA template, enhancing R-loop formation and cRNA retention at heterochromatin.
Language	English
Publishing date	2024-04-24
Publishing country	United States
Document type	Journal Article
ZDB-ID	2649101-1
ISSN	2211-1247 ; 2211-1247
ISSN (online)	2211-1247
ISSN	2211-1247
DOI	10.1016/j.celrep.2024.114137
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Article ; Online: The E3-ligases SCFPpa and APC/CCdh1 co-operate to regulate CENP-ACID expression across the cell cycle.

Moreno-Moreno, Olga / Torras-Llort, Mònica / Azorin, Fernando

Nucleic acids research

2019 Volume 47, Issue 7, Page(s) 3395–3406

Abstract: Centromere identity is determined by the specific deposition of CENP-A, a histone H3 variant localizing exclusively at centromeres. Increased CENP-A expression, which is a frequent event in cancer, causes mislocalization, ectopic kinetochore assembly and ...

Abstract	Centromere identity is determined by the specific deposition of CENP-A, a histone H3 variant localizing exclusively at centromeres. Increased CENP-A expression, which is a frequent event in cancer, causes mislocalization, ectopic kinetochore assembly and genomic instability. Proteolysis regulates CENP-A expression and prevents its misincorporation across chromatin. How proteolysis restricts CENP-A localization to centromeres is not well understood. Here we report that, in Drosophila, CENP-ACID expression levels are regulated throughout the cell cycle by the combined action of SCFPpa and APC/CCdh1. We show that SCFPpa regulates CENP-ACID expression in G1 and, importantly, in S-phase preventing its promiscuous incorporation across chromatin during replication. In G1, CENP-ACID expression is also regulated by APC/CCdh1. We also show that Cal1, the specific chaperone that deposits CENP-ACID at centromeres, protects CENP-ACID from SCFPpa-mediated degradation but not from APC/CCdh1-mediated degradation. These results suggest that, whereas SCFPpa targets the fraction of CENP-ACID that is not in complex with Cal1, APC/CCdh1 mediates also degradation of the Cal1-CENP-ACID complex and, thus, likely contributes to the regulation of centromeric CENP-ACID deposition.
MeSH term(s)	Anaphase-Promoting Complex-Cyclosome/metabolism ; Animals ; Cdh1 Proteins/metabolism ; Cell Cycle ; Cell Line ; Centromere/metabolism ; Centromere Protein A/metabolism ; Drosophila Proteins/metabolism ; Drosophila melanogaster/cytology ; Drosophila melanogaster/enzymology ; Drosophila melanogaster/metabolism ; G1 Phase ; S Phase ; Ubiquitin-Protein Ligases/metabolism
Chemical Substances	Cal1 protein, Drosophila ; Cdh1 Proteins ; Centromere Protein A ; Drosophila Proteins ; Anaphase-Promoting Complex-Cyclosome (EC 2.3.2.27) ; Ubiquitin-Protein Ligases (EC 2.3.2.27)
Language	English
Publishing date	2019-01-01
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	186809-3
ISSN	1362-4962 ; 1362-4954 ; 0301-5610 ; 0305-1048
ISSN (online)	1362-4962 ; 1362-4954
ISSN	0301-5610 ; 0305-1048
DOI	10.1093/nar/gkz060
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Article ; Online: Baf-mediated transcriptional regulation of teashirt is essential for the development of neural progenitor cell lineages.

Ko, Byung Su / Han, Myeong Hoon / Kwon, Min Jee / Cha, Dong Gon / Ji, Yuri / Park, Eun Seo / Jeon, Min Jae / Kim, Somi / Lee, Kyeongho / Choi, Yoon Ha / Lee, Jusung / Torras-Llort, Monica / Yoon, Ki-Jun / Lee, Hyosang / Kim, Jong Kyoung / Lee, Sung Bae

Experimental & molecular medicine

2024 Volume 56, Issue 2, Page(s) 422–440

Abstract: Accumulating evidence hints heterochromatin anchoring to the inner nuclear membrane as an upstream regulatory process of gene expression. Given that the formation of neural progenitor cell lineages and the subsequent maintenance of postmitotic neuronal ... ...

Abstract	Accumulating evidence hints heterochromatin anchoring to the inner nuclear membrane as an upstream regulatory process of gene expression. Given that the formation of neural progenitor cell lineages and the subsequent maintenance of postmitotic neuronal cell identity critically rely on transcriptional regulation, it seems possible that the development of neuronal cells is influenced by cell type-specific and/or context-dependent programmed regulation of heterochromatin anchoring. Here, we explored this possibility by genetically disrupting the evolutionarily conserved barrier-to-autointegration factor (Baf) in the Drosophila nervous system. Through single-cell RNA sequencing, we demonstrated that Baf knockdown induces prominent transcriptomic changes, particularly in type I neuroblasts. Among the differentially expressed genes, our genetic analyses identified teashirt (tsh), a transcription factor that interacts with beta-catenin, to be closely associated with Baf knockdown-induced phenotypes that were suppressed by the overexpression of tsh or beta-catenin. We also found that Baf and tsh colocalized in a region adjacent to heterochromatin in type I NBs. Notably, the subnuclear localization pattern remained unchanged when one of these two proteins was knocked down, indicating that both proteins contribute to the anchoring of heterochromatin to the inner nuclear membrane. Overall, this study reveals that the Baf-mediated transcriptional regulation of teashirt is a novel molecular mechanism that regulates the development of neural progenitor cell lineages.
MeSH term(s)	Animals ; beta Catenin ; Drosophila ; Gene Expression Regulation ; Heterochromatin/genetics ; Neural Stem Cells ; Thyrotropin
Chemical Substances	beta Catenin ; Heterochromatin ; Thyrotropin (9002-71-5) ; BAF protein, Drosophila ; tsh protein, Drosophila (135315-85-4)
Language	English
Publishing date	2024-02-19
Publishing country	United States
Document type	Journal Article
ZDB-ID	1328915-9
ISSN	2092-6413 ; 1226-3613 ; 0378-8512
ISSN (online)	2092-6413
ISSN	1226-3613 ; 0378-8512
DOI	10.1038/s12276-024-01169-3
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Article ; Online: Variations on a nucleosome theme: The structural basis of centromere function.

Moreno-Moreno, Olga / Torras-Llort, Mònica / Azorín, Fernando

BioEssays : news and reviews in molecular, cellular and developmental biology

2017 Volume 39, Issue 4

Abstract: The centromere is a specialized chromosomal structure that dictates kinetochore assembly and, thus, is essential for accurate chromosome segregation. Centromere identity is determined epigenetically by the presence of a centromere-specific histone H3 ... ...

Abstract	The centromere is a specialized chromosomal structure that dictates kinetochore assembly and, thus, is essential for accurate chromosome segregation. Centromere identity is determined epigenetically by the presence of a centromere-specific histone H3 variant, CENP-A, that replaces canonical H3 in centromeric chromatin. Here, we discuss recent work by Roulland et al. that identifies structural elements of the nucleosome as essential determinants of centromere function. In particular, CENP-A nucleosomes have flexible DNA ends due to the short αN helix of CENP-A. The higher flexibility of the DNA ends of centromeric nucleosomes impairs binding of linker histones H1, while it facilitates binding of other essential centromeric proteins, such as CENP-C, and is required for mitotic fidelity. This work extends previous observations indicating that the differential structural properties of CENP-A nucleosomes are on the basis of its contribution to centromere identity and function. Here, we discuss the implications of this work and the questions arising from it.
Language	English
Publishing date	2017-04
Publishing country	United States
Document type	Journal Article ; Review
ZDB-ID	50140-2
ISSN	1521-1878 ; 0265-9247
ISSN (online)	1521-1878
ISSN	0265-9247
DOI	10.1002/bies.201600241
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Article ; Online: A fraction of barrier-to-autointegration factor (BAF) associates with centromeres and controls mitosis progression.

Torras-Llort, Mònica / Medina-Giró, Sònia / Escudero-Ferruz, Paula / Lipinszki, Zoltan / Moreno-Moreno, Olga / Karman, Zoltan / Przewloka, Marcin R / Azorín, Fernando

Communications biology

2020 Volume 3, Issue 1, Page(s) 454

Abstract: Barrier-to-Autointegration Factor (BAF) is a conserved nuclear envelope (NE) component that binds chromatin and helps its anchoring to the NE. Cycles of phosphorylation and dephosphorylation control BAF function. Entering mitosis, phosphorylation ... ...

Abstract	Barrier-to-Autointegration Factor (BAF) is a conserved nuclear envelope (NE) component that binds chromatin and helps its anchoring to the NE. Cycles of phosphorylation and dephosphorylation control BAF function. Entering mitosis, phosphorylation releases BAF from chromatin and facilitates NE-disassembly. At mitotic exit, PP2A-mediated dephosphorylation restores chromatin binding and nucleates NE-reassembly. Here, we show that in Drosophila a small fraction of BAF (cenBAF) associates with centromeres. We also find that PP4 phosphatase, which is recruited to centromeres by CENP-C, prevents phosphorylation and release of cenBAF during mitosis. cenBAF is necessary for proper centromere assembly and accurate chromosome segregation, being critical for mitosis progression. Disrupting cenBAF localization prevents PP2A inactivation in mitosis compromising global BAF phosphorylation, which in turn leads to its persistent association with chromatin, delays anaphase onset and causes NE defects. These results suggest that, together with PP4 and CENP-C, cenBAF forms a centromere-based mechanism that controls chromosome segregation and mitosis progression.
MeSH term(s)	Animals ; Biomarkers ; Centromere/genetics ; Centromere/metabolism ; Chromatin/genetics ; Chromatin/metabolism ; DNA-Binding Proteins/genetics ; DNA-Binding Proteins/metabolism ; Drosophila Proteins/genetics ; Drosophila Proteins/metabolism ; Fluorescent Antibody Technique ; Gene Expression Regulation ; Mitosis ; Models, Biological ; Nuclear Proteins/genetics ; Nuclear Proteins/metabolism ; Phosphorylation ; Protein Binding ; Protein Transport
Chemical Substances	BAF protein, Drosophila ; Biomarkers ; Chromatin ; DNA-Binding Proteins ; Drosophila Proteins ; Nuclear Proteins
Language	English
Publishing date	2020-08-19
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	2399-3642
ISSN (online)	2399-3642
DOI	10.1038/s42003-020-01182-y
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Article ; Online: Focus on the centre: the role of chromatin on the regulation of centromere identity and function.

Torras-Llort, Mònica / Moreno-Moreno, Olga / Azorín, Fernando

The EMBO journal

2009 Volume 28, Issue 16, Page(s) 2337–2348

Abstract: The centromere is a specialised chromosomal structure that regulates faithful chromosome segregation during cell division, as it dictates the site of assembly of the kinetochore, a critical structure that mediates binding of chromosomes to the spindle, ... ...

Abstract	The centromere is a specialised chromosomal structure that regulates faithful chromosome segregation during cell division, as it dictates the site of assembly of the kinetochore, a critical structure that mediates binding of chromosomes to the spindle, monitors bipolar attachment and pulls chromosomes to the poles during anaphase. Identified more than a century ago as the primary constriction of condensed metaphase chromosomes, the centromere remained elusive to molecular characterisation for many years owed to its unusual enrichment in highly repetitive satellite DNA sequences, except in budding yeast. In the last decade, our understanding of centromere structure, organisation and function has increased tremendously. Nowadays, we know that centromere identity is determined epigenetically by the formation of a unique type of chromatin, which is characterised by the presence of the centromere-specific histone H3 variant CenH3, originally called CENP-A, which replaces canonical histone H3 at centromeres. CenH3-chromatin constitutes the physical and functional foundation for kinetochore assembly. This review explores recent studies addressing the structural and functional characterisation of CenH3-chromatin, its assembly and propagation during mitosis, and its contribution to kinetochore assembly.
MeSH term(s)	Amino Acid Sequence ; Animals ; Autoantigens/analysis ; Autoantigens/chemistry ; Autoantigens/genetics ; Autoantigens/metabolism ; Centromere/chemistry ; Centromere/genetics ; Centromere/metabolism ; Centromere Protein A ; Chromatin/chemistry ; Chromatin/genetics ; Chromatin/metabolism ; Chromosomal Proteins, Non-Histone/analysis ; Chromosomal Proteins, Non-Histone/chemistry ; Chromosomal Proteins, Non-Histone/genetics ; Chromosomal Proteins, Non-Histone/metabolism ; Epigenesis, Genetic ; Humans ; Molecular Sequence Data ; Sequence Alignment
Chemical Substances	Autoantigens ; CENPA protein, human ; Centromere Protein A ; Chromatin ; Chromosomal Proteins, Non-Histone
Language	English
Publishing date	2009-07-23
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	586044-1
ISSN	1460-2075 ; 0261-4189
ISSN (online)	1460-2075
ISSN	0261-4189
DOI	10.1038/emboj.2009.174
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Zs.A 1808: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (1.OG) ab Jg. 2022: Lesesaal (EG)
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Article: Functional characterization of the human phosphodiesterase 7A1 promoter.

Torras-Llort, Mònica / Azorín, Fernando

The Biochemical journal

2003 Volume 373, Issue Pt 3, Page(s) 835–843

Abstract: In this paper, the human phosphodiesterase 7A1 (h PDE7A1 ) promoter region was identified and functionally characterized. Transient transfection experiments indicated that a 2.9 kb fragment of the h PDE7A1 5'-flanking region, to position -2907, has ... ...

Abstract	In this paper, the human phosphodiesterase 7A1 (h PDE7A1 ) promoter region was identified and functionally characterized. Transient transfection experiments indicated that a 2.9 kb fragment of the h PDE7A1 5'-flanking region, to position -2907, has strong promoter activity in Jurkat T-cells. Deletion analysis showed that the proximal region, up to position -988, contains major cis -regulatory elements of the h PDE7A1 promoter. This minimal promoter region contains a regulatory CpG island which is essential for promoter activity. The CpG island contains three potential cAMP-response-element-binding protein (CREB)-binding sites that, as judged by in vivo dimethyl sulphate (DMS) footprinting, are occupied in Jurkat T-cells. Moreover, over-expression of CREB results in increased promoter activity, but, on the other hand, promoter activity decreases when a dominant-negative form of CREB (KCREB) is over-expressed. In vivo DMS footprinting strongly indicates that other transcription factors, such Ets-2, nuclear factor of activated T-cells 1 (NFAT-1) and nuclear factor kappaB (NF-kappaB), might also contribute to the regulation of h PDE7A1 promoter. Finally, h PDE7A1 promoter was found to be induced by treatment with PMA, but not by treatment with dibutyryl cAMP or forskolin. These results provide insights into the factors and mechanisms that regulate expression of the h PDE7A gene.
MeSH term(s)	3',5'-Cyclic-AMP Phosphodiesterases/chemistry ; 3',5'-Cyclic-AMP Phosphodiesterases/genetics ; 3',5'-Cyclic-AMP Phosphodiesterases/metabolism ; Amino Acid Sequence ; Base Sequence ; Binding Sites ; Cloning, Molecular ; Colforsin/pharmacology ; CpG Islands ; Cyclic AMP Response Element-Binding Protein/metabolism ; Cyclic Nucleotide Phosphodiesterases, Type 7 ; DNA Footprinting ; DNA, Complementary ; Humans ; Molecular Sequence Data ; Promoter Regions, Genetic ; Tetradecanoylphorbol Acetate/pharmacology
Chemical Substances	Cyclic AMP Response Element-Binding Protein ; DNA, Complementary ; Colforsin (1F7A44V6OU) ; 3',5'-Cyclic-AMP Phosphodiesterases (EC 3.1.4.17) ; Cyclic Nucleotide Phosphodiesterases, Type 7 (EC 3.1.4.17) ; PDE7A protein, human (EC 3.1.4.17) ; Tetradecanoylphorbol Acetate (NI40JAQ945)
Language	English
Publishing date	2003-08-01
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2969-5
ISSN	1470-8728 ; 0264-6021 ; 0006-2936 ; 0306-3275
ISSN (online)	1470-8728
ISSN	0264-6021 ; 0006-2936 ; 0306-3275
DOI	10.1042/BJ20021829
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Article ; Online: Proteolysis restricts localization of CID, the centromere-specific histone H3 variant of Drosophila, to centromeres.

Moreno-Moreno, Olga / Torras-Llort, Mònica / Azorín, Fernando

Nucleic acids research

2006 Volume 34, Issue 21, Page(s) 6247–6255

Abstract: Centromere identity is determined by the formation of a specialized chromatin structure containing the centromere-specific histone H3 variant CENP-A. The precise molecular mechanism(s) accounting for the specific deposition of CENP-A at centromeres are ... ...

Abstract	Centromere identity is determined by the formation of a specialized chromatin structure containing the centromere-specific histone H3 variant CENP-A. The precise molecular mechanism(s) accounting for the specific deposition of CENP-A at centromeres are still poorly understood. Centromeric deposition of CENP-A, which is independent of DNA replication, might involve specific chromatin assembly complexes and/or specific interactions with kinetochore components. However, transiently expressed CENP-A incorporates throughout chromatin indicating that CENP-A nucleosomes can also be promiscuously deposited during DNA replication. Therefore, additional mechanisms must exist to prevent deposition of CENP-A nucleosomes during replication and/or to remove them afterwards. Here, using transient expression experiments performed in Drosophila Kc cells, we show that proteasome-mediated degradation restricts localization of Drosophila CENP-A (CID) to centromeres by eliminating mislocalized CID as well as by regulating available CID levels. Regulating available CID levels appears essential to ensure centromeric deposition of transiently expressed CID as, when expression is increased in the presence of proteasome inhibitors, newly synthesized CID mislocalizes. Mislocalization of CID affects cell cycle progression as a high percentage of cells showing mislocalized CID are reactive against alphaPSer(10)H3 antibodies, enter mitosis at a very low frequency and show strong segregation defects. However, cells showing reduced amounts of mislocalized CID show normal cell cycle progression.
MeSH term(s)	Animals ; Cell Cycle ; Cells, Cultured ; Centromere/chemistry ; Centromere Protein A ; Chromatin/chemistry ; Cysteine Proteinase Inhibitors/pharmacology ; DNA-Binding Proteins/analysis ; DNA-Binding Proteins/metabolism ; Drosophila Proteins/analysis ; Drosophila Proteins/metabolism ; Drosophila melanogaster/cytology ; Drosophila melanogaster/enzymology ; Drosophila melanogaster/genetics ; Histones/analysis ; Histones/metabolism ; Leupeptins/pharmacology ; Proteasome Endopeptidase Complex/metabolism ; Proteasome Inhibitors
Chemical Substances	Centromere Protein A ; Chromatin ; Cid protein, Drosophila ; Cysteine Proteinase Inhibitors ; DNA-Binding Proteins ; Drosophila Proteins ; Histones ; Leupeptins ; Proteasome Inhibitors ; Proteasome Endopeptidase Complex (EC 3.4.25.1) ; benzyloxycarbonylleucyl-leucyl-leucine aldehyde (RF1P63GW3K)
Language	English
Publishing date	2006
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2205588-5
ISSN	1362-4962 ; 1746-8272 ; 0305-1048 ; 0261-3166
ISSN (online)	1362-4962 ; 1746-8272
ISSN	0305-1048 ; 0261-3166
DOI	10.1093/nar/gkl902
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Article ; Online: The F box protein partner of paired regulates stability of Drosophila centromeric histone H3, CenH3(CID).

Moreno-Moreno, Olga / Medina-Giró, Sònia / Torras-Llort, Mònica / Azorín, Fernando

Current biology : CB

2011 Volume 21, Issue 17, Page(s) 1488–1493

Abstract: Centromere identity and function is determined by the specific localization of CenH3 (reviewed in [1-7]). Several mechanisms regulate centromeric CenH3 localization, including proteasome-mediated degradation that, both in budding yeast and Drosophila, ... ...

Abstract	Centromere identity and function is determined by the specific localization of CenH3 (reviewed in [1-7]). Several mechanisms regulate centromeric CenH3 localization, including proteasome-mediated degradation that, both in budding yeast and Drosophila, regulates CenH3 levels and prevents promiscuous misincorporation throughout chromatin [8, 9]. CenH3(CENP-A) proteolysis has also been reported in senescent human cells [10] or upon infection with herpes simplex virus 1 [11]. Little is known, however, about the actual mechanisms that regulate CenH3 proteolysis. Recent work in budding yeast identified Psh1 as an E3-ubiquitin ligase that mediates degradation of CenH3(Cse4p) [12, 13], but E3-ligases regulating CenH3 stability in metazoans are unknown. Here, we report that the F box protein partner of paired (Ppa), which is a variable subunit of the main E3-ligase SCF [14-17], mediates CenH3(CID) stability in Drosophila. Our results show that Ppa depletion results in increased CenH3(CID) levels. Ppa physically interacts with CenH3(CID) through the CATD(CID) that, in the fly, mediates Ppa-dependent CenH3(CID) stability. Altogether, these results strongly suggest that, in Drosophila, SCF(Ppa) regulates CenH3(CID) proteolysis. Interestingly, most known SCF complexes are inactive when, at mitosis, de novo CenH3(CID) deposition takes place at centromeres, suggesting that, in Drosophila, CenH3(CID) deposition and proteolysis are synchronized events.
MeSH term(s)	Animals ; Carrier Proteins/genetics ; Carrier Proteins/metabolism ; Cathepsins/metabolism ; Centromere/chemistry ; Chromatin/chemistry ; Drosophila/cytology ; Drosophila/genetics ; Drosophila/metabolism ; Drosophila Proteins/genetics ; Drosophila Proteins/metabolism ; Endopeptidases/genetics ; Endopeptidases/metabolism ; Histones/genetics ; Histones/metabolism ; Microscopy, Fluorescence ; Mitosis ; Proteolysis
Chemical Substances	Carrier Proteins ; Chromatin ; Drosophila Proteins ; Histones ; Ppa protein, Drosophila ; Cathepsins (EC 3.4.-) ; Endopeptidases (EC 3.4.-) ; Prosbeta2 protein, Drosophila (EC 3.4.-) ; Prosbeta6 protein, Drosophila (EC 3.4.-)
Language	English
Publishing date	2011-08-25
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1071731-6
ISSN	1879-0445 ; 0960-9822
ISSN (online)	1879-0445
ISSN	0960-9822
DOI	10.1016/j.cub.2011.07.041
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