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  • 1
    Keywords: Germany ; IN-VIVO ; SUPPORT ; GENE ; GENOME ; PROTEIN ; PROTEINS ; RNA ; TIME ; DNA ; FAMILY ; SUFFICIENT ; STAGE ; Drosophila ; MELANOGASTER ; DNA methylation ; EMBRYO ; FISSION YEAST ; METHYLTRANSFERASE ACTIVITY ; OVEREXPRESSION ; METHYLATION ; CATALYTIC ACTIVITY ; CYTOSINE-5 METHYLTRANSFERASES ; DE-NOVO METHYLATION ; DNA methylation,Drosophila,DNA methyltransferase,Dnmt2,Su(var)3-9 ; DNA methyltransferase ; EMBRYONIC STEM-CELLS ; EMBRYOS ; HISTONE H3 METHYLTRANSFERASE ; HYPERMETHYLATION ; LETHALITY ; MAMMALIAN DEVELOPMENT ; METHYLTRANSFERASE GENE ; SEQUENCE SPECIFICITY
    Abstract: The methylation status of Drosophila DNA has been discussed controversially over a long time. Recent evidence has provided strong support for the existence of 5-methylcytosine in DNA preparations from embryonic stages of fly development. The Drosophila genome contains a single candidate DNA methyltransferase gene that has been termed Dnmt2. This gene belongs to a widely conserved family of putative DNA methyltransferases. However, no catalytic activity has been demonstrated for any Dnmt2-like protein yet. We have now established a protocol for the immunological detection of methylated cytosine in fly embryos. Confocal analysis of immunostained embryos provided direct evidence for the methylation of embryonic DNA. In order to analyse the function of Dnmt2 in DNA methylation, we depleted the protein by RNA interference. Depletion of Dnmt2 had no detectable effect on embryonic development and resulted in a complete loss of DNA methylation. Consistently, overexpression of Dnmt2 from an inducible transgene resulted in significant genomic hypermethylation at CpT and CpA dinucleotides. These results demonstrate that Dnmt2 is both necessary and sufficient for DNA methylation in Drosophila and suggest a novel CpT/A-specific DNA methyltransferase activity for Dnmt2 proteins
    Type of Publication: Journal article published
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  • 2
    Keywords: GENOME ; RELEASE ; DELETION ; ELEMENT ; Drosophila ; DROSOPHILA-MELANOGASTER ; MELANOGASTER ; ELEMENTS ; genetics ; DELETIONS ; REGION ; REGIONS ; DUPLICATION ; SELECTION ; heredity ; DEFICIENCY ; USA ; SET ; LOCI ; INSERTION ; DUPLICATIONS ; BAR LOCUS ; UNEQUAL CROSSING-OVER
    Abstract: We describe a second-gene ration deficiency kit for Drosophila melanogaster composed of molecularly mapped deletions on an isogenic background, covering similar to 77% of the Release 5.1 genome. Using a previously reported collection of FRT-bearing P-element insertions, we have generated 655 new deletions and verified a set of 209 deletion-bearing fly stocks. In addition to deletions, we demonstrate how the P elements may also be used to generate a set of custom inversions and duplications, particularly useful for balancing difficult regions of the genome carrying haplo-insufficient loci. We describe a simple computational resource that facilitates selection of appropriate elements for generating custom deletions. Finally, we provide a computational resource that facilitates selection of other mapped FRT-bearing elements that, when combined with the DrosDel collection, can theoretically generate over half a million precisely mapped deletions
    Type of Publication: Journal article published
    PubMed ID: 17720900
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  • 3
    Keywords: EXPRESSION ; Germany ; REQUIREMENTS ; Drosophila ; MELANOGASTER ; EMBRYO ; LOCALIZATION ; EMBRYOS ; Drosophila melanogaster,pole cell migration,gonad formation,Scribble1,scribble,discs-large 1,lethal ; GERM-CELL MIGRATION ; NEUROTACTIN
    Type of Publication: Journal article published
    PubMed ID: 12711540
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  • 4
    Keywords: Germany ; SYSTEM ; GENE ; GENES ; GENOME ; GENOME SEQUENCE ; PROTEIN ; PROTEINS ; DNA ; MECHANISM ; SEQUENCE ; SEQUENCES ; DIFFERENCE ; Drosophila ; DROSOPHILA-MELANOGASTER ; MELANOGASTER ; REQUIRES ; DE-NOVO ; EMBRYONIC STEM-CELLS ; METHYLTRANSFERASE ; ANOPHELES-GAMBIAE ; DNA methylation,DNA methyltransferase,Dnmt2,Drosophila,Anopheles ; HUMAN DNMT2 ; MOUSE CELLS
    Abstract: DNA methylation is a central mechanism of epigenetic regulation. Whereas vertebrate DNA methylation requires at least four different DNA methyltransferases, Drosophila melanogaster only utilizes a single, Dnmt2-like enzyme. This profound difference has raised the question of the evolutionary significance of the Drosophila methylation system. We have now identified Dnmt2-like open reading frames in the genome sequences of Drosophila pseudoobscura and Anopheles gambiae. These genes represent the only candidate DNA methyltransferases in their respective genomes. Consistent with a catalytic activity of Dnmt2 proteins, we could also demonstrate low but significant levels of DNA methylation in genomic DNA from these species. Lastly, we were also able to detect highly conserved Dnmt2-like open reading frames and concomitant DNA methylation in several additional Drosophila species, which suggests that Dnmt2-mediated DNA methylation has been conserved over a considerable evolutionary distance
    Type of Publication: Journal article published
    PubMed ID: 15056358
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  • 5
    Keywords: GENE ; MELANOGASTER ; BINDING-PROTEIN ; CHAPERONE ; REACTION CYCLE ; INTERACTION NETWORK ; IMAGINAL DISCS ; HUMAN TRANSCRIPTION MACHINERY ; R2TP COMPLEX ; 2ND CHROMOSOME
    Abstract: The R2TP is a recently identified Hsp90 co-chaperone, composed of four proteins as follows: Pih1D1, RPAP3, and the AAA(+)-ATPases RUVBL1 and RUVBL2. In mammals, the R2TP is involved in the biogenesis of cellular machineries such as RNA polymerases, small nucleolar ribonucleoparticles and phosphatidylinositol 3-kinase-related kinases. Here, we characterize the spaghetti (spag) gene of Drosophila, the homolog of human RPAP3. This gene plays an essential function during Drosophila development. We show that Spag protein binds Drosophila orthologs of R2TP components and Hsp90, like its yeast counterpart. Unexpectedly, Spag also interacts and stimulates the chaperone activity of Hsp70. Using null mutants and flies with inducible RNAi, we show that spaghetti is necessary for the stabilization of snoRNP core proteins and target of rapamycin activity and likely the assembly of RNA polymerase II. This work highlights the strong conservation of both the HSP90/R2TP system and its clients and further shows that Spag, unlike Saccharomyces cerevisiae Tah1, performs essential functions in metazoans. Interaction of Spag with both Hsp70 and Hsp90 suggests a model whereby R2TP would accompany clients from Hsp70 to Hsp90 to facilitate their assembly into macromolecular complexes.
    Type of Publication: Journal article published
    PubMed ID: 24394412
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  • 6
    Keywords: Germany ; INFORMATION ; SYSTEM ; GENE ; GENOME ; PROTEIN ; PROTEINS ; COMPLEX ; COMPLEXES ; DNA ; FAMILY ; BINDING ; ASSOCIATION ; FORM ; ISOFORM ; IDENTIFICATION ; SUBUNIT ; Drosophila ; COMPONENT ; DNA methylation ; EMBRYO ; BINDING-PROTEINS ; REPLICATION ; SUBUNITS ; INTERACTS ; INSIGHTS ; METHYLATION ; TRANSCRIPTIONAL REPRESSION ; ARCHITECTURE ; EMBRYOS ; BINDING PROTEIN ; molecular ; BINDING-PROTEIN ; RE ; HOMOLOGY ; interaction ; OCT ; MBD2/3 ; MECP2 ; MI-2 ; NURD ; DEACETYLASE ; DROSOPHILA GENOME ; GENE-REGULATION ; HISTONE DEACETYLASE COMPLEX ; histone modification ; MI-2/NURD ; NUCLEOSOME
    Abstract: Background: Methyl-DNA binding proteins help to translate epigenetic information encoded by DNA methylation into covalent histone modifications. MBD2/3 is the only candidate gene in the Drosophila genome with extended homologies to mammalian MBD2 and MBD3 proteins, which represent a co-repressor and an integral component of the Nucleosome Remodelling and Deacetylase ( NuRD) complex, respectively. An association of Drosophila MBD2/3 with the Drosophila NuRD complex has been suggested previously. We have now analyzed the molecular interactions between MBD2/3 and the NuRD complex in greater detail. Results: The two MBD2/3 isoforms precisely cofractionated with NuRD proteins during gel filtration of extracts derived from early and late embryos. In addition, we demonstrate that MBD2/3 forms multimers, and engages in specific interactions with the p55 and MI-2 subunits of the Drosophila NuRD complex. Conclusion: Our data provide novel insights into the association between Drosophila MBD2/3 and NuRD proteins. Additionally, this work provides a first analysis of the architecture of the Drosophila NuRD complex
    Type of Publication: Journal article published
    PubMed ID: 15516265
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  • 7
    Keywords: Germany ; GENE ; GENOME ; PROTEIN ; PROTEINS ; COMPLEX ; COMPLEXES ; DNA ; BINDING ; SUPPRESSION ; chromosome ; MUTANT ; CHROMATIN ; Drosophila ; MELANOGASTER ; MUTATION ; DNA methylation ; EMBRYO ; LOCALIZATION ; INSIGHTS ; CHROMATIN STRUCTURE ; METHYLATION ; TRANSCRIPTIONAL REPRESSION ; EMBRYOS ; HISTONE H3 METHYLTRANSFERASE ; BINDING PROTEIN ; F ; BINDING-PROTEIN ; SUBSET ; PATTERN ; ALLELE ; HOMOLOGY ; DEFECTS ; ARABIDOPSIS ; CPG-BINDING-PROTEINS ; DEACETYLASE COMPLEX ; DMI-2 ; HETEROCHROMATIN ; MBD2/3 ; MECP2 ; MI-2 ; NURD
    Abstract: Methyl-DNA binding proteins play an important role in epigenetic gene regulation. The Drosophila genome encodes a single protein (MBD2/3) with extended homologies to the vertebrate methyl-DNA binding proteins MBD2 and MBD3. However, very little is known about its functional properties. We have now characterized an MBD2/3 null mutant allele that is viable and fertile. This mutation caused a strong dominant suppression of position-effect variegation and also resulted in a high rate of chromosome segregation defects during early embryogenesis. Confocal analysis of mutant embryos showed local displacement of MI-2 from DNA and indicated that MBD2/3 is associated with only a subset of MI-2 complexes. In addition, band shift experiments demonstrated a specific binding of MBD2/3 to CpT/A-methylated DNA, which reflects the endogenous DNA methylation pattern of Drosophila. Consistently, the localization of MBD2/3 was disrupted in embryos with reduced levels of DNA methylation. Our data provide novel insights into the function of MBD2/3 proteins and strongly suggest the existence of methylation-dependent chromatin structures in Drosophila
    Type of Publication: Journal article published
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  • 8
    Keywords: CELLS ; EXPRESSION ; GROWTH ; CELL ; Germany ; SITE ; GENE ; GENE-EXPRESSION ; GENOME ; PROTEIN ; RNA ; DIFFERENTIATION ; ACTIVATION ; CYCLE ; REPAIR ; STABILITY ; OVEREXPRESSION ; METHYLATION ; NUCLEOTIDE EXCISION-REPAIR ; RE ; HUMAN CANCER ; ARABIDOPSIS ; PROMOTES
    Abstract: DNA methylation is an epigenetic modification that is essential for gene silencing and genome stability in many organisms. Although methyltransferases that promote DNA methylation are well characterized, the molecular mechanism underlying active DNA demethylation is poorly understood and controversial(1,2). Here we show that Gadd45a ( growth arrest and DNA-damage-inducible protein 45 alpha), a nuclear protein involved in maintenance of genomic stability, DNA repair and suppression of cell growth 3,4, has a key role in active DNA demethylation. Gadd45a overexpression activates methylation-silenced reporter plasmids and promotes global DNA demethylation. Gadd45a knockdown silences gene expression and leads to DNA hypermethylation. During active demethylation of oct4 in Xenopus laevis oocytes(5), Gadd45a is specifically recruited to the site of demethylation. Active demethylation occurs by DNA repair and Gadd45a interacts with and requires the DNA repair endonuclease XPG. We conclude that Gadd45a relieves epigenetic gene silencing by promoting DNA repair, which erases methylation marks
    Type of Publication: Journal article published
    PubMed ID: 17268471
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  • 9
    Keywords: CANCER ; CANCER CELLS ; CELLS ; CELL ; prognosis ; PHOSPHORYLATION ; PROGRESSION ; ABERRATIONS ; DAMAGE ; LOCALIZATION ; XENOPUS ; RECRUITMENT ; DUPLICATION ; REPLICATION ; CDK2-CYCLIN ; AURORA-A ; MAINTENANCE ; DNA-DAMAGE RESPONSE
    Abstract: Centrosomes are central regulators of mitosis that are often amplified in cancer cells. Centrosomes function both as organizers of the mitotic spindle and as reaction centers to trigger activation of Cdk1 and G(2)/M transition in the cell cycle, but their functional organization remains incomplete. Recent proteomic studies have identified novel components of the human centrosome including Cep63, a protein of unknown function that Xenopus studies have implicated in mitotic spindle assembly and spindle inactivation after DNA damage. Here, we report that human Cep63 binds to and recruits Cdk1 to centrosomes, and thereby regulates mitotic entry. RNAi-mediated Cep63 depletion in U2OS cancer cells induced polyploidization through mitotic skipping. Elicitation of this phenotype was associated with downregulation of centrosomal Cdk1, mimicking the phenotype induced by direct depletion of Cdk1. In contrast, Cep63 overexpression induced de novo centrosome amplification during cell-cycle interphase. Induction of this phenotype was suppressible by cell treatment with the Cdk inhibitor roscovitine. In a survey of 244 neuroblastoma cases, Cep63 mRNA overexpression was associated with MYCN oncogene amplification and poor prognosis. In cultured cells, Cep63 overexpression was associated with an enhancement in replication-induced DNA breakage. Together, our findings define human Cep63 as a centrosomal recruitment factor for Cdk1 that is essential for mitotic entry, providing a physical link between the centrosome and the cell-cycle machinery.
    Type of Publication: Journal article published
    PubMed ID: 21406398
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  • 10
    Keywords: DNA-METHYLATION ; Germany ; CELL ; DNA ; BIOLOGY ; DNA methylation ; METHYLATION
    Type of Publication: Meeting abstract published
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