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Article ; Online: Chromatin dynamics coupled to DNA repair.

Huertas, Dori / Sendra, Ramon / Muñoz, Purificación

Epigenetics

2009 Volume 4, Issue 1, Page(s) 31–42

Abstract: In order to protect and preserve the integrity of the genome, eukaryotic cells have developed accurate DNA repair pathways involving a coordinated network of DNA repair and epigenetic factors. The DNA damage response has to proceed in the context of ... ...

Abstract	In order to protect and preserve the integrity of the genome, eukaryotic cells have developed accurate DNA repair pathways involving a coordinated network of DNA repair and epigenetic factors. The DNA damage response has to proceed in the context of chromatin, a packaged and compact structure that is flexible enough to regulate the accession of the DNA repair machinery to DNA-damaged sites. Chromatin modifications and ATP-remodeling activities are both necessary to ensure efficient DNA repair. Here we review the current progress of research into the importance of chromatin modifications and the ATP-remodeling complex to the DNA damage response, with respect to the sensing and signaling of DNA lesions, DNA repair and the processes that restore chromatin structure.
MeSH term(s)	Adenosine Triphosphate/chemistry ; Animals ; Chromatin/chemistry ; Chromatin/genetics ; Chromatin/metabolism ; Chromatin Assembly and Disassembly ; Chromosomes/ultrastructure ; DNA Breaks, Double-Stranded ; DNA Damage ; DNA Repair ; Drosophila melanogaster/metabolism ; Histones/metabolism ; Humans ; Models, Biological ; Protein Structure, Tertiary ; Saccharomyces cerevisiae/metabolism
Chemical Substances	Chromatin ; H2AX protein, human ; Histones ; Adenosine Triphosphate (8L70Q75FXE)
Language	English
Publishing date	2009-01-31
Publishing country	United States
Document type	Journal Article ; Review
ISSN	1559-2308
ISSN (online)	1559-2308
DOI	10.4161/epi.4.1.7733
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Article: Drosophila vigilin, DDP1, localises to the cytoplasm and associates to the rough endoplasmic reticulum.

Batlle, Marta / Marsellach, Francesc-Xavier / Huertas, Dori / Azorín, Fernando

Biochimica et biophysica acta

2011 Volume 1809, Issue 1, Page(s) 46–55

Abstract: Functional characterisation of vigilin, a highly conserved multi-KH-domain protein that binds RNA and ssDNA, remains elusive and, to some extent, controversial. Studies performed in Saccharomyces cerevisiae and human cells indicate that vigilin localises ...

Abstract	Functional characterisation of vigilin, a highly conserved multi-KH-domain protein that binds RNA and ssDNA, remains elusive and, to some extent, controversial. Studies performed in Saccharomyces cerevisiae and human cells indicate that vigilin localises to the cytoplasm, binds ribosomes, associates to RER and regulates mRNA translation. On the other hand, we and others reported a contribution to heterochromatin-mediated gene silencing (PEV) and chromosome segregation in S. cerevisiae, Drosophila and human cells. Whether this contribution is direct remains, however, unclear. Here, we report that Drosophila vigilin, DDP1, vastly localises to the cytoplasm, being largely excluded from the nucleus. We also show that DDP1 preferentially associates to RER and co-purifies with several ribosomal proteins, suggesting a contribution to mRNA translation. In light of these results, the contribution of DDP1 to PEV was re-examined. Here, we show that a newly generated null ddp1(Δ) mutation is only a weak suppressor of PEV, which is in contrast with our own previous results showing dominant suppression in the presence of a strong hypomorphic ddp1(15.1) mutation. Similar results were obtained in the fission yeast Schizosaccharomyces pombe, where vigilin (Vgl1) also associates to RER, having no significant contribution to PEV at centromeres, telomeres and the mating-type locus. Altogether, these results indicate that cytoplasmic localisation and association to RER, but not contribution to heterochromatin organisation, are evolutionarily conserved features of vigilin, favouring a model by which vigilin acts in the cytoplasm, regulating RNA metabolism, and affects nuclear functions only indirectly.
MeSH term(s)	Animals ; Animals, Genetically Modified ; Blotting, Western ; Cells, Cultured ; Cytoplasm/metabolism ; DNA-Binding Proteins/genetics ; DNA-Binding Proteins/metabolism ; Drosophila Proteins/genetics ; Drosophila Proteins/metabolism ; Drosophila melanogaster/cytology ; Drosophila melanogaster/genetics ; Drosophila melanogaster/metabolism ; Embryo, Nonmammalian/embryology ; Embryo, Nonmammalian/metabolism ; Endoplasmic Reticulum, Rough/metabolism ; Endoplasmic Reticulum, Rough/ultrastructure ; Female ; Green Fluorescent Proteins/genetics ; Green Fluorescent Proteins/metabolism ; Heterochromatin/genetics ; Heterochromatin/metabolism ; Histones/metabolism ; Immunohistochemistry ; Lysine/metabolism ; Male ; Methylation ; Microscopy, Immunoelectron ; Mutation ; Protein Binding ; RNA Interference ; RNA-Binding Proteins/genetics ; RNA-Binding Proteins/metabolism ; Ribosomal Proteins/metabolism ; Schizosaccharomyces/genetics ; Schizosaccharomyces/metabolism ; Schizosaccharomyces pombe Proteins/genetics ; Schizosaccharomyces pombe Proteins/metabolism
Chemical Substances	DNA-Binding Proteins ; Dp1 protein, Drosophila ; Drosophila Proteins ; Heterochromatin ; Histones ; RNA-Binding Proteins ; Ribosomal Proteins ; Schizosaccharomyces pombe Proteins ; Vgl1 protein, S pombe ; Green Fluorescent Proteins (147336-22-9) ; high density lipoprotein binding protein (147605-06-9) ; Lysine (K3Z4F929H6)
Language	English
Publishing date	2011-01
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	60-7
ISSN	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
ISSN (online)	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650
ISSN	0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
DOI	10.1016/j.bbagrm.2010.10.005
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Article ; Online: Inhibition of Gsk3b Reduces Nfkb1 Signaling and Rescues Synaptic Activity to Improve the Rett Syndrome Phenotype in Mecp2-Knockout Mice.

Jorge-Torres, Olga C / Szczesna, Karolina / Roa, Laura / Casal, Carme / Gonzalez-Somermeyer, Louisa / Soler, Marta / Velasco, Cecilia D / Martínez-San Segundo, Pablo / Petazzi, Paolo / Sáez, Mauricio A / Delgado-Morales, Raúl / Fourcade, Stephane / Pujol, Aurora / Huertas, Dori / Llobet, Artur / Guil, Sonia / Esteller, Manel

Cell reports

2018 Volume 23, Issue 6, Page(s) 1665–1677

Abstract: Rett syndrome (RTT) is the second leading cause of mental impairment in girls and is currently untreatable. RTT is caused, in more than 95% of cases, by loss-of-function mutations in the methyl CpG-binding protein 2 gene (MeCP2). We propose here a ... ...

Abstract	Rett syndrome (RTT) is the second leading cause of mental impairment in girls and is currently untreatable. RTT is caused, in more than 95% of cases, by loss-of-function mutations in the methyl CpG-binding protein 2 gene (MeCP2). We propose here a molecular target involved in RTT: the glycogen synthase kinase-3b (Gsk3b) pathway. Gsk3b activity is deregulated in Mecp2-knockout (KO) mice models, and SB216763, a specific inhibitor, is able to alleviate the clinical symptoms with consequences at the molecular and cellular levels. In vivo, inhibition of Gsk3b prolongs the lifespan of Mecp2-KO mice and reduces motor deficits. At the molecular level, SB216763 rescues dendritic networks and spine density, while inducing changes in the properties of excitatory synapses. Gsk3b inhibition can also decrease the nuclear activity of the Nfkb1 pathway and neuroinflammation. Altogether, our findings indicate that Mecp2 deficiency in the RTT mouse model is partially rescued following treatment with SB216763.
MeSH term(s)	Animals ; Biomarkers/metabolism ; Cells, Cultured ; Cerebellum/metabolism ; Cerebellum/pathology ; Dendritic Spines/drug effects ; Dendritic Spines/metabolism ; Dendritic Spines/pathology ; Disease Models, Animal ; Glycogen Synthase Kinase 3 beta/antagonists & inhibitors ; Glycogen Synthase Kinase 3 beta/metabolism ; Humans ; Indoles/pharmacology ; Inflammation/pathology ; Longevity ; Maleimides/pharmacology ; Methyl-CpG-Binding Protein 2/deficiency ; Methyl-CpG-Binding Protein 2/metabolism ; Mice, Inbred C57BL ; Mice, Knockout ; NF-kappa B p50 Subunit/metabolism ; Phenotype ; Protein Kinase Inhibitors/pharmacology ; Rett Syndrome/metabolism ; Rett Syndrome/pathology ; Signal Transduction ; Survival Analysis ; Synapses/metabolism ; Up-Regulation/drug effects
Chemical Substances	Biomarkers ; Indoles ; Maleimides ; Mecp2 protein, mouse ; Methyl-CpG-Binding Protein 2 ; NF-kappa B p50 Subunit ; Protein Kinase Inhibitors ; SB 216763 ; Nfkb1 protein, mouse (147257-52-1) ; Glycogen Synthase Kinase 3 beta (EC 2.7.11.1)
Language	English
Publishing date	2018-05-09
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2649101-1
ISSN	2211-1247 ; 2211-1247
ISSN (online)	2211-1247
ISSN	2211-1247
DOI	10.1016/j.celrep.2018.04.010
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Article: The multi-KH domain protein of Saccharomyces cerevisiae Scp160p contributes to the regulation of telomeric silencing.

Marsellach, Francesc-Xavier / Huertas, Dori / Azorín, Fernando

The Journal of biological chemistry

2006 Volume 281, Issue 26, Page(s) 18227–18235

Abstract: Multi-KH domain proteins are highly evolutionarily conserved proteins that associate to polyribosomes and participate in RNA metabolism. Recent evidence indicates that multi-KH domain proteins also contribute to the structural organization of ... ...

Abstract	Multi-KH domain proteins are highly evolutionarily conserved proteins that associate to polyribosomes and participate in RNA metabolism. Recent evidence indicates that multi-KH domain proteins also contribute to the structural organization of heterochromatin both in mammals and Drosophila. Here, we show that the multi-KH domain protein of Saccharomyces cerevisiae, Scp160p, contributes to silencing at telomeres and at the mating-type locus, but not to ribosomal silencing. The contribution of Scp160p to silencing is independent of its binding to the ribosome as deletion of the last two KH domains, which mediate ribosomal binding, has no effect on silencing. Disruption of SCP160 increases cell ploidy but this effect is also independent of the contribution of Scp160p to telomeric silencing as strong relief of silencing is observed in Deltascp160 cells with normal ploidy and, vice versa, Deltascp160 cells with highly increased ploidy show no significant silencing defects. The TPE phenotype of Deltascp160 cells associates to a decreased Sir3p deposition at telomeres and, in good agreement, silencing is rescued by SIR3 overexpression and in a Deltarif1Deltarif2 mutant. Scp160p shows a distinct perinuclear localization that is independent of its ability to bind ribosomes. Moreover, telomere clustering at the nuclear envelope is perturbed in Deltascp160 cells and disruption of the histone deacetylase RPD3, which is known to improve telomere clustering, rescues telomeric silencing in Deltascp160 cells. These results are discussed in the context of a model in which Scp160p contributes to silencing by helping telomere clustering.
MeSH term(s)	Cell Nucleus/physiology ; Chromosome Segregation ; Gene Deletion ; Gene Expression Regulation, Fungal ; Gene Silencing ; Membrane Proteins/chemistry ; Membrane Proteins/genetics ; Membrane Proteins/metabolism ; Nuclear Proteins/chemistry ; Nuclear Proteins/genetics ; Nuclear Proteins/metabolism ; Protein Structure, Tertiary ; RNA-Binding Proteins ; Ribosomes/physiology ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae Proteins/chemistry ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism ; Telomere/physiology
Chemical Substances	Membrane Proteins ; Nuclear Proteins ; RNA-Binding Proteins ; SCP160 protein, S cerevisiae ; Saccharomyces cerevisiae Proteins
Language	English
Publishing date	2006-04-21
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.M601671200
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Article ; Online: Dysregulation of the long non-coding RNA transcriptome in a Rett syndrome mouse model.

Petazzi, Paolo / Sandoval, Juan / Szczesna, Karolina / Jorge, Olga C / Roa, Laura / Sayols, Sergi / Gomez, Antonio / Huertas, Dori / Esteller, Manel

RNA biology

2013 Volume 10, Issue 7, Page(s) 1197–1203

Abstract: Mecp2 is a transcriptional repressor protein that is mutated in Rett syndrome, a neurodevelopmental disorder that is the second most common cause of mental retardation in women. It has been shown that the loss of the Mecp2 protein in Rett syndrome cells ... ...

Abstract	Mecp2 is a transcriptional repressor protein that is mutated in Rett syndrome, a neurodevelopmental disorder that is the second most common cause of mental retardation in women. It has been shown that the loss of the Mecp2 protein in Rett syndrome cells alters the transcriptional silencing of coding genes and microRNAs. Herein, we have studied the impact of Mecp2 impairment in a Rett syndrome mouse model on the global transcriptional patterns of long non-coding RNAs (lncRNAs). Using a microarray platform that assesses 41,232 unique lncRNA transcripts, we have identified the aberrant lncRNA transcriptome that is present in the brain of Rett syndrome mice. The study of the most relevant lncRNAs altered in the assay highlighted the upregulation of the AK081227 and AK087060 transcripts in Mecp2-null mice brains. Chromatin immunoprecipitation demonstrated the Mecp2 occupancy in the 5'-end genomic loci of the described lncRNAs and its absence in Rett syndrome mice. Most importantly, we were able to show that the overexpression of AK081227 mediated by the Mecp2 loss was associated with the downregulation of its host coding protein gene, the gamma-aminobutyric acid receptor subunit Rho 2 (Gabrr2). Overall, our findings indicate that the transcriptional dysregulation of lncRNAs upon Mecp2 loss contributes to the neurological phenotype of Rett syndrome and highlights the complex interaction between ncRNAs and coding-RNAs.
MeSH term(s)	5' Flanking Region ; Animals ; Cluster Analysis ; Disease Models, Animal ; Female ; Gene Expression Profiling ; Gene Expression Regulation ; Genetic Loci ; Humans ; Male ; Methyl-CpG-Binding Protein 2/genetics ; Methyl-CpG-Binding Protein 2/metabolism ; Mice ; Mice, Knockout ; Protein Binding ; RNA, Long Noncoding/genetics ; Reproducibility of Results ; Rett Syndrome/genetics ; Transcriptome
Chemical Substances	Methyl-CpG-Binding Protein 2 ; RNA, Long Noncoding
Language	English
Publishing date	2013-04-17
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	1555-8584
ISSN (online)	1555-8584
DOI	10.4161/rna.24286
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Article ; Online: Whole exome sequencing of Rett syndrome-like patients reveals the mutational diversity of the clinical phenotype.

Lucariello, Mario / Vidal, Enrique / Vidal, Silvia / Saez, Mauricio / Roa, Laura / Huertas, Dori / Pineda, Mercè / Dalfó, Esther / Dopazo, Joaquin / Jurado, Paola / Armstrong, Judith / Esteller, Manel

Human genetics

2016 Volume 135, Issue 12, Page(s) 1343–1354

Abstract: Classical Rett syndrome (RTT) is a neurodevelopmental disorder where most of cases carry MECP2 mutations. Atypical RTT variants involve mutations in CDKL5 and FOXG1. However, a subset of RTT patients remains that do not carry any mutation in the ... ...

Abstract	Classical Rett syndrome (RTT) is a neurodevelopmental disorder where most of cases carry MECP2 mutations. Atypical RTT variants involve mutations in CDKL5 and FOXG1. However, a subset of RTT patients remains that do not carry any mutation in the described genes. Whole exome sequencing was carried out in a cohort of 21 female probands with clinical features overlapping with those of RTT, but without mutations in the customarily studied genes. Candidates were functionally validated by assessing the appearance of a neurological phenotype in Caenorhabditis elegans upon disruption of the corresponding ortholog gene. We detected pathogenic variants that accounted for the RTT-like phenotype in 14 (66.6 %) patients. Five patients were carriers of mutations in genes already known to be associated with other syndromic neurodevelopmental disorders. We determined that the other patients harbored mutations in genes that have not previously been linked to RTT or other neurodevelopmental syndromes, such as the ankyrin repeat containing protein ANKRD31 or the neuronal acetylcholine receptor subunit alpha-5 (CHRNA5). Furthermore, worm assays demonstrated that mutations in the studied candidate genes caused locomotion defects. Our findings indicate that mutations in a variety of genes contribute to the development of RTT-like phenotypes.
MeSH term(s)	Adolescent ; Adult ; Animals ; Caenorhabditis elegans/genetics ; Carrier Proteins/genetics ; Child ; Child, Preschool ; DNA Mutational Analysis ; Exome/genetics ; Female ; Forkhead Transcription Factors/genetics ; Genetic Variation ; High-Throughput Nucleotide Sequencing ; Humans ; Methyl-CpG-Binding Protein 2/genetics ; Mutation ; Nerve Tissue Proteins/genetics ; Protein-Serine-Threonine Kinases/genetics ; Receptors, Nicotinic/genetics ; Rett Syndrome/genetics ; Rett Syndrome/physiopathology
Chemical Substances	ANKRD31 protein, human ; CHRNA5 protein, human ; Carrier Proteins ; FOXG1 protein, human ; Forkhead Transcription Factors ; MECP2 protein, human ; Methyl-CpG-Binding Protein 2 ; Nerve Tissue Proteins ; Receptors, Nicotinic ; Protein-Serine-Threonine Kinases (EC 2.7.11.1) ; CDKL5 protein, human (EC 2.7.11.22)
Language	English
Publishing date	2016-12
Publishing country	Germany
Document type	Journal Article
ZDB-ID	223009-4
ISSN	1432-1203 ; 0340-6717
ISSN (online)	1432-1203
ISSN	0340-6717
DOI	10.1007/s00439-016-1721-3
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Article ; Online: Circadian cycle-dependent MeCP2 and brain chromatin changes.

Martínez de Paz, Alexia / Sanchez-Mut, Jose Vicente / Samitier-Martí, Mireia / Petazzi, Paolo / Sáez, Mauricio / Szczesna, Karolina / Huertas, Dori / Esteller, Manel / Ausió, Juan

PloS one

2015 Volume 10, Issue 4, Page(s) e0123693

Abstract: Methyl CpG binding protein 2 (MeCP2) is a chromosomal protein of the brain, very abundant especially in neurons, where it plays an important role in the regulation of gene expression. Hence it has the potential to be affected by the mammalian circadian ... ...

Abstract	Methyl CpG binding protein 2 (MeCP2) is a chromosomal protein of the brain, very abundant especially in neurons, where it plays an important role in the regulation of gene expression. Hence it has the potential to be affected by the mammalian circadian cycle. We performed expression analyses of mice brain frontal cortices obtained at different time points and we found that the levels of MeCP2 are altered circadianly, affecting overall organization of brain chromatin and resulting in a circadian-dependent regulation of well-stablished MeCP2 target genes. Furthermore, this data suggests that alterations of MeCP2 can be responsible for the sleeping disorders arising from pathological stages, such as in autism and Rett syndrome.
MeSH term(s)	Animals ; Brain/metabolism ; CLOCK Proteins/metabolism ; Cerebral Cortex/metabolism ; Chromatin/metabolism ; Circadian Rhythm/genetics ; Gene Expression Regulation, Developmental ; Methyl-CpG-Binding Protein 2/metabolism ; Mice ; Mice, Inbred C57BL ; Promoter Regions, Genetic/genetics
Chemical Substances	Chromatin ; Methyl-CpG-Binding Protein 2 ; CLOCK Proteins (EC 2.3.1.48)
Language	English
Publishing date	2015-04-13
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	1932-6203
ISSN (online)	1932-6203
DOI	10.1371/journal.pone.0123693
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Article: Drosophila DDP1, a multi-KH-domain protein, contributes to centromeric silencing and chromosome segregation.

Huertas, Dori / Cortés, Alfred / Casanova, Jordi / Azorín, Fernando

Current biology : CB

2004 Volume 14, Issue 18, Page(s) 1611–1620

Abstract: Background: The Drosophila melanogaster DDP1 protein is a highly evolutionarily conserved protein that is characterised by the presence of 15 tandemly organized KH domains, known for mediating high-affinity binding to single-stranded nucleic acids (RNA ... ...

Abstract	Background: The Drosophila melanogaster DDP1 protein is a highly evolutionarily conserved protein that is characterised by the presence of 15 tandemly organized KH domains, known for mediating high-affinity binding to single-stranded nucleic acids (RNA and ssDNA). Consistent with its molecular organization, DDP1 binds single-stranded nucleic acids with high affinity, in vitro. It was shown earlier that, in polytene chromosomes, DDP1 is found in association with chromocenter heterochromatin, suggesting a contribution to heterochromatin formation and/or maintenance. Results: In this paper, the actual contribution of DDP1 to the structural and functional properties of heterochromatin was determined through the analysis of the phenotypes associated with the hypomorphic ddp1(15.1) mutation that was generated through the mobilization of a P element inserted in the second intron of ddp1. ddp1(15.1) behaves as a dominant suppressor of PEV in the variegated rearrangement In(1)w(m4) as well as in several transgenic lines showing variegated expression of a hsp70-white(+) transgene. In polytene chromosomes from homozygous ddp1(15.1) larvae, histone H3-K9 methylation and HP1 deposition at chromocentre heterochromatin are strongly reduced. Our results also show that, when the maternal contribution of DDP1 is reduced, chromosome condensation and segregation are compromised. Moreover, in a ddp1(15.1) mutant background, transmission of the nonessential Dp1187 minichromosome is reduced. Conclusions: We conclude that DDP1 contributes to the structural and functional properties of heterochromatin. These results are discussed in the context of current models for the formation and maintenance of heterochromatin; in these models, HP1 deposition depends on H3-K9 methylation that, in turn, requires the contribution of the RNAi pathway.
MeSH term(s)	Animals ; Animals, Genetically Modified ; Centromere/physiology ; Chromosomal Proteins, Non-Histone/metabolism ; Chromosome Segregation/physiology ; Crosses, Genetic ; DNA-Binding Proteins/genetics ; DNA-Binding Proteins/metabolism ; DNA-Binding Proteins/physiology ; Drosophila Proteins/genetics ; Drosophila Proteins/metabolism ; Drosophila Proteins/physiology ; Drosophila melanogaster/metabolism ; Fluorescent Antibody Technique ; Heterochromatin/physiology ; Histones/metabolism ; Methylation ; Models, Biological ; Mutation/genetics ; Protein Structure, Tertiary ; RNA Interference
Chemical Substances	Chromosomal Proteins, Non-Histone ; DNA-Binding Proteins ; Dp1 protein, Drosophila ; Drosophila Proteins ; Heterochromatin ; Histones ; heterochromatin protein 1, Drosophila
Language	English
Publishing date	2004-09-21
Publishing country	England
Document type	Comparative Study ; 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.2004.09.024
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Article: Drosophila vigilin, DDP1, localises to the cytoplasm and associates to the rough endoplasmic reticulum

Batlle, Marta / Marsellach, Francesc-Xavier / Huertas, Dori / Azorín, Fernando

BBA - Gene Regulatory Mechanisms. 2011 Jan., v. 1809, no. 1

2011

Abstract	Functional characterisation of vigilin, a highly conserved multi-KH-domain protein that binds RNA and ssDNA, remains elusive and, to some extent, controversial. Studies performed in Saccharomyces cerevisiae and human cells indicate that vigilin localises to the cytoplasm, binds ribosomes, associates to RER and regulates mRNA translation. On the other hand, we and others reported a contribution to heterochromatin-mediated gene silencing (PEV) and chromosome segregation in S. cerevisiae, Drosophila and human cells. Whether this contribution is direct remains, however, unclear. Here, we report that Drosophila vigilin, DDP1, vastly localises to the cytoplasm, being largely excluded from the nucleus. We also show that DDP1 preferentially associates to RER and co-purifies with several ribosomal proteins, suggesting a contribution to mRNA translation. In light of these results, the contribution of DDP1 to PEV was re-examined. Here, we show that a newly generated null ddp1Δ mutation is only a weak suppressor of PEV, which is in contrast with our own previous results showing dominant suppression in the presence of a strong hypomorphic ddp1¹⁵.¹ mutation. Similar results were obtained in the fission yeast Schizosaccharomyces pombe, where vigilin (Vgl1) also associates to RER, having no significant contribution to PEV at centromeres, telomeres and the mating-type locus. Altogether, these results indicate that cytoplasmic localisation and association to RER, but not contribution to heterochromatin organisation, are evolutionarily conserved features of vigilin, favouring a model by which vigilin acts in the cytoplasm, regulating RNA metabolism, and affects nuclear functions only indirectly.
Keywords	Drosophila ; Saccharomyces cerevisiae ; Schizosaccharomyces pombe ; centromeres ; chromosome segregation ; gene silencing ; heterochromatin ; humans ; loci ; messenger RNA ; metabolism ; models ; mutation ; ribosomal proteins ; ribosomes ; rough endoplasmic reticulum ; single-stranded DNA ; telomeres ; translation (genetics)
Language	English
Dates of publication	2011-01
Size	p. 46-55.
Publishing place	Elsevier B.V.
Document type	Article
ZDB-ID	2406725-8
ISSN	1876-4320 ; 1874-9399
ISSN (online)	1876-4320
ISSN	1874-9399
DOI	10.1016/j.bbagrm.2010.10.005
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Article ; Online: Circadian cycle-dependent MeCP2 and brain chromatin changes.

Alexia Martínez de Paz / Jose Vicente Sanchez-Mut / Mireia Samitier-Martí / Paolo Petazzi / Mauricio Sáez / Karolina Szczesna / Dori Huertas / Manel Esteller / Juan Ausió

PLoS ONE, Vol 10, Iss 4, p e

2015 Volume 0123693

Abstract	Methyl CpG binding protein 2 (MeCP2) is a chromosomal protein of the brain, very abundant especially in neurons, where it plays an important role in the regulation of gene expression. Hence it has the potential to be affected by the mammalian circadian cycle. We performed expression analyses of mice brain frontal cortices obtained at different time points and we found that the levels of MeCP2 are altered circadianly, affecting overall organization of brain chromatin and resulting in a circadian-dependent regulation of well-stablished MeCP2 target genes. Furthermore, this data suggests that alterations of MeCP2 can be responsible for the sleeping disorders arising from pathological stages, such as in autism and Rett syndrome.
Keywords	Medicine ; R ; Science ; Q
Language	English
Publishing date	2015-01-01T00:00:00Z
Publisher	Public Library of Science (PLoS)
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Order via subito

Inter-library loan at ZB MED

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In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

Order via subito

Full text online

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Kategorien

Inter-library loan at ZB MED