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  • 1
    Electronic Resource
    Electronic Resource
    Marking time (2006)
    [s.l.] : Nature Publishing Group
    Nature genetics 38 (2006), S. 276-277 
    Details
    ISSN: 1546-1718
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Medicine
    Notes: [Auszug] Some of us are early birds, and others are night owls—in other words, each of us has times of day when we're not at our best. That's because everyone has a biological clock that generates a circadian rhythm. Circadian rhythm refers to the cyclical physiological and behavioral changes in cells ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/ng0306-276
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  • 2
    Electronic Resource
    Electronic Resource
    The trithorax-group gene in Drosophila little imaginal discs encodes a trimethylated histone H3 Lys4 demethylase (2007)
    [s.l.] : Nature Publishing Group
    Nature structural & molecular biology 14 (2007), S. 344-346 
    Details
    ISSN: 1545-9985
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Medicine
    Notes: [Auszug] Histone H3 Lys4 (H3K4) is methylated by yeast Set1–COMPASS and its mammalian homolog, the MLL complex. Human JARID1d can demethylate trimethyl-H3K4 (H3K4me3). We identified Drosophila melanogaster little imaginal discs (Lid) as the JARID1d homolog. We report that Lid knockdown using RNA ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/nsmb1217
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  • 3
    Electronic Resource
    Electronic Resource
    Molecular biology Antagonizing the neighbours (2005)
    [s.l.] : Nature Publishing Group
    Nature 438 (2005), S. 1090-1091 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Crack open any cell nucleus and look inside: you'll see what look like beads on a string. The beads are nucleosomes, small protein complexes that help to package the DNA (the strings) into the cramped confines of the nucleus. In the past fifteen years, nucleosomes have graduated in our ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/4381090a
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  • 4
    Electronic Resource
    Electronic Resource
    In vivo assay for protein-protein interactions using Drosophila chromosomes (1996)
    Springer
    Chromosoma 104 (1996), S. 393-404 
    Details
    ISSN: 1432-0886
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract The ability of a chimeric HP1-Polycomb (Pc) protein to bind both to heterochromatin and to euchromatic sites of Pc protein binding was exploited to detect stable protein-protein interactions in vivo. Previously, we showed that endogenous Pc protein was recruited to ectopic heterochromatic binding sites by the chimeric protein. Here, we examine the association of other Pc group (Pc-G) proteins. We show that Posterior sex combs (Psc) protein also is recruited to heterochromatin by the chimeric protein, demonstrating that Psc protein participates in direct protein-protein interaction with Pc protein or Pc-associated protein. In flies carrying temperature-sensitive alleles of Enhancer of zeste[E(z)] the general decondensation of polytene chromosomes that occurs at the restrictive temperature is associated with loss of binding of endogenous Pc and chimeric HP1-Polycomb protein to euchromatin, but binding of HP1 and chimeric HP1-Polycomb protein to the heterochromatin is maintained. The E(z) mutation also results in the loss of chimera-dependent binding to heterochromatin by endogenous Pc and Psc proteins at the restrictive temperature, suggesting that interaction of these proteins is mediated by E(z) protein. A myc-tagged full-length Suppressor 2 of zeste [Su(z)2] protein interacts poorly or not at all with ectopic Pc-G complexes, but a truncated Su(z)2 protein is strongly recruited to all sites of chimeric protein binding. Trithorax protein is not recruited to the heterochromatin by the chimeric HP1-Polycomb protein, suggesting either that this protein does not interact directly with Pc-G complexes or that such interactions are regulated. Ectopic binding of chimeric chromosomal proteins provides a useful tool for distinguishing specific protein-protein interactions from specific protein-DNA interactions important for complex assembly in vivo.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00352263
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  • 5
    Electronic Resource
    Electronic Resource
    In vivo assay for protein-protein interactions using Drosophila chromosomes (1996)
    Springer
    Chromosoma 104 (1996), S. 393-404 
    Details
    ISSN: 1432-0886
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract. The ability of a chimeric HP1-Polycomb (Pc) protein to bind both to heterochromatin and to euchromatic sites of Pc protein binding was exploited to detect stable protein-protein interactions in vivo. Previously, we showed that endogenous Pc protein was recruited to ectopic heterochromatic binding sites by the chimeric protein. Here, we examine the association of other Pc group (Pc-G) proteins. We show that Posterior sex combs (Psc) protein also is recruited to heterochromatin by the chimeric protein, demonstrating that Psc protein participates in direct protein-protein interaction with Pc protein or Pc-associated protein. In flies carrying temperature-sensitive alleles of Enhancer of zeste[E(z)] the general decondensation of polytene chromosomes that occurs at the restrictive temperature is associated with loss of binding of endogenous Pc and chimeric HP1-Polycomb protein to euchromatin, but binding of HP1 and chimeric HP1-Polycomb protein to the heterochromatin is maintained. The E(z) mutation also results in the loss of chimera-dependent binding to heterochromatin by endogenous Pc and Psc proteins at the restrictive temperature, suggesting that interaction of these proteins is mediated by E(z) protein. A myc-tagged full-length Suppressor 2 of zeste [Su(z)2] protein interacts poorly or not at all with ectopic Pc-G complexes, but a truncated Su(z)2 protein is strongly recruited to all sites of chimeric protein binding. Trithorax protein is not recruited to the heterochromatin by the chimeric HP1-Polycomb protein, suggesting either that this protein does not interact directly with Pc-G complexes or that such interactions are regulated. Ectopic binding of chimeric chromosomal proteins provides a useful tool for distinguishing specific protein-protein interactions from specific protein-DNA interactions important for complex assembly in vivo.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00352263
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  • 6
    Electronic Resource
    Electronic Resource
    A heat shock-activated cDNA rescues the recessive lethality of mutations in the heterochromatin-associated protein HP1 of Drosophila melanogaster (1993)
    Springer
    Molecular genetics and genomics 240 (1993), S. 333-338 
    Details
    ISSN: 1617-4623
    Keywords: Heterochromatin protein 1 ; Position-effect variegation ; P element ; Drosophila melanogaster
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract HP1 is a small nonhistone chromosomal protein of Drosophila melanogaster predominantly localized to the pericentric heterochromatin. We have shown previously that mutations in the HP1 coding sequences are associated with dominant suppression of heterochromatic position-effect variegation, and with recessive lethality. When fused to an Hsp70 heat shock gene promoter, the cDNA encoding HP1 supports the heat shock-inducible accumulation of HPI protein in transgenic flies; this cDNA construct complements the dominant suppression of position-effect variegation associated with mutations in the HP1 gene. Here, we report experiments demonstrating that the heat shock-driven HP1 cDNA is capable of fully rescuing the recessive lethality associated with HP1 mutations in a heat shock-dependent fashion. If heat shock-induced HP1 expression is delayed for as long as 5 days, more than half of the mutant flies still survive until adulthood, consistent with a substantial maternal contribution to embryonic and larval viability. Elevating HP1 levels as late as 7–8 days of development is sufficient to enhance variegation three-fold, suggesting that the extent of heterochromatic position effect can be modified subsequent to the initial appearance of HP1 in the nuclei of syncytial blastoderm embryos.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00280383
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  • 7
    Electronic Resource
    Electronic Resource
    Reaching for New Heitz (2000)
    Springer
    Genetica 109 (2000), S. 7-8 
    Details
    ISSN: 1573-6857
    Keywords: heterochromatin ; nucleosome
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1026532032454
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  • 8
    Electronic Resource
    Electronic Resource
    Versatility of Conviction: Heterochromatin as Both a Repressor and an Activator of Transcription (2000)
    Springer
    Genetica 109 (2000), S. 19-24 
    Details
    ISSN: 1573-6857
    Keywords: chromosomal proteins ; Drosophila ; heterochromatin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1026544717126
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  • 9
    Electronic Resource
    Electronic Resource
    Introduction Shedding New Light on the Dark Corners of the Nucleus (2000)
    Springer
    Genetica 109 (2000), S. 3-6 
    Details
    ISSN: 1573-6857
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1026545800287
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  • 10
    Electronic Resource
    Electronic Resource
    Position effect variegation in Drosophila: Towards a genetics of chromatin assembly (1989)
    New York, NY : Wiley-Blackwell
    BioEssays 11 (1989), S. 14-17 
    Details
    ISSN: 0265-9247
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The formation of a highly condensed chromosome structure (heterochromatin) in a region of a eukaryotic chromosome can inactivate the genes within that region. Genetic studies using the fruitfly Drosophila melanogaster have identified several essential genes which influence the formation of heterochromatin. My purpose in this review is to summarize some recent work on the genetics of heterochromatin assembly in Drosophila and a recent model for how chromosomal proteins may interact to form a heterochromatic structure.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bies.950110105
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