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  • 1
    Online Resource
    Online Resource
    Histone H3.3 is enriched in covalent modifications associated with active chromatin
    Proceedings of the National Academy of Sciences ; 2004
    In:  Proceedings of the National Academy of Sciences Vol. 101, No. 6 ( 2004-02-10), p. 1525-1530
    Details
    In: Proceedings of the National Academy of Sciences, Proceedings of the National Academy of Sciences, Vol. 101, No. 6 ( 2004-02-10), p. 1525-1530
    Abstract: Chromatin states can be distinguished by differential covalent modifications of histones or by utilization of histone variants. Chromatin associated with transcriptionally active loci becomes enriched for histones with particular lysine modifications and accumulates the H3.3 histone variant, the substrate for replication-independent nucleosome assembly. However, studies of modifications at particular loci have not distinguished between histone variants, so the relationship among modifications, histone variants, and nucleosome assembly pathways is unclear. To address this uncertainty, we have quantified the relative abundance of H3 and H3.3 and their lysine modifications. Using a Drosophila cell line system in which H3.3 has been shown to specifically package active loci, we found that H3.3 accounts for ≈25% of total histone 3 in bulk chromatin, enough to package essentially all actively transcribed genes. MS and antibody characterization of separated histone 3 fractions revealed that H3.3 is relatively enriched in modifications associated with transcriptional activity and deficient in dimethyl lysine-9, which is abundant in heterochromatin. To explain enrichment on alternative variants, we propose that histone modifications are tied to the alternative nucleosome assembly pathways that use primarily H3 at replication forks and H3.3 at actively transcribed genes in a replication-independent manner.
    Type of Medium: Online Resource
    ISSN: 0027-8424 , 1091-6490
    URL: Article
    DOI: 10.1073/pnas.0308092100
    RVK:
    TA 1000
    RVK:
    WA 15000
    Language: English
    Publisher: Proceedings of the National Academy of Sciences
    Publication Date: 2004
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  • 2
    Online Resource
    Online Resource
    Histone variants, nucleosome assembly and epigenetic inheritance
    Elsevier BV ; 2004
    In:  Trends in Genetics Vol. 20, No. 7 ( 2004-7), p. 320-326
    Details
    In: Trends in Genetics, Elsevier BV, Vol. 20, No. 7 ( 2004-7), p. 320-326
    Type of Medium: Online Resource
    ISSN: 0168-9525
    URL: Article
    DOI: 10.1016/j.tig.2004.05.004
    RVK:
    WA 15000
    Language: English
    Publisher: Elsevier BV
    Publication Date: 2004
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  • 3
    Online Resource
    Online Resource
    Modulation of a Transcription Factor Counteracts Heterochromatic Gene Silencing in Drosophila
    Elsevier BV ; 2001
    In:  Cell Vol. 104, No. 6 ( 2001-03), p. 839-847
    Details
    In: Cell, Elsevier BV, Vol. 104, No. 6 ( 2001-03), p. 839-847
    Type of Medium: Online Resource
    ISSN: 0092-8674
    URL: Article
    DOI: 10.1016/S0092-8674(01)00281-1
    RVK:
    XA 36269
    RVK:
    WA 15000
    Language: English
    Publisher: Elsevier BV
    Publication Date: 2001
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    SSG: 12
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  • 4
    Online Resource
    Online Resource
    Epigenetic Consequences of Nucleosome Dynamics
    Elsevier BV ; 2002
    In:  Cell Vol. 111, No. 3 ( 2002-11), p. 281-284
    Details
    In: Cell, Elsevier BV, Vol. 111, No. 3 ( 2002-11), p. 281-284
    Type of Medium: Online Resource
    ISSN: 0092-8674
    URL: Article
    DOI: 10.1016/S0092-8674(02)01081-4
    RVK:
    XA 36269
    RVK:
    WA 15000
    Language: English
    Publisher: Elsevier BV
    Publication Date: 2002
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    detail.hit.zdb_id: 2001951-8
    SSG: 12
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  • 5
    Online Resource
    Online Resource
    Centromeres Are Specialized Replication Domains in Heterochromatin
    Rockefeller University Press ; 2001
    In:  The Journal of Cell Biology Vol. 153, No. 1 ( 2001-04-02), p. 101-110
    Details
    In: The Journal of Cell Biology, Rockefeller University Press, Vol. 153, No. 1 ( 2001-04-02), p. 101-110
    Abstract: The properties that define centromeres in complex eukaryotes are poorly understood because the underlying DNA is normally repetitive and indistinguishable from surrounding noncentromeric sequences. However, centromeric chromatin contains variant H3-like histones that may specify centromeric regions. Nucleosomes are normally assembled during DNA replication; therefore, we examined replication and chromatin assembly at centromeres in Drosophila cells. DNA in pericentric heterochromatin replicates late in S phase, and so centromeres are also thought to replicate late. In contrast to expectation, we show that centromeres replicate as isolated domains early in S phase. These domains do not appear to assemble conventional H3-containing nucleosomes, and deposition of the Cid centromeric H3-like variant proceeds by a replication-independent pathway. We suggest that late-replicating pericentric heterochromatin helps to maintain embedded centromeres by blocking conventional nucleosome assembly early in S phase, thereby allowing the deposition of centromeric histones.
    Type of Medium: Online Resource
    ISSN: 0021-9525 , 1540-8140
    URL: Article
    DOI: 10.1083/jcb.153.1.101
    RVK:
    WA 15000
    Language: English
    Publisher: Rockefeller University Press
    Publication Date: 2001
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  • 6
    Online Resource
    Online Resource
    The Centromere Paradox: Stable Inheritance with Rapidly Evolving DNA
    American Association for the Advancement of Science (AAAS) ; 2001
    In:  Science Vol. 293, No. 5532 ( 2001-08-10), p. 1098-1102
    Details
    In: Science, American Association for the Advancement of Science (AAAS), Vol. 293, No. 5532 ( 2001-08-10), p. 1098-1102
    Abstract: Every eukaryotic chromosome has a centromere, the locus responsible for poleward movement at mitosis and meiosis. Although conventional loci are specified by their DNA sequences, current evidence favors a chromatin-based inheritance mechanism for centromeres. The chromosome segregation machinery is highly conserved across all eukaryotes, but the DNA and protein components specific to centromeric chromatin are evolving rapidly. Incompatibilities between rapidly evolving centromeric components may be responsible for both the organization of centromeric regions and the reproductive isolation of emerging species.
    Type of Medium: Online Resource
    ISSN: 0036-8075 , 1095-9203
    URL: Article
    DOI: 10.1126/science.1062939
    RVK:
    TA 1000
    RVK:
    WA 15000
    Language: English
    Publisher: American Association for the Advancement of Science (AAAS)
    Publication Date: 2001
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    SSG: 11
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  • 7
    Online Resource
    Online Resource
    The End in Sight
    Elsevier BV ; 2004
    In:  Molecular Cell Vol. 15, No. 4 ( 2004-08), p. 494-495
    Details
    In: Molecular Cell, Elsevier BV, Vol. 15, No. 4 ( 2004-08), p. 494-495
    Type of Medium: Online Resource
    ISSN: 1097-2765
    URL: Article
    DOI: 10.1016/j.molcel.2004.08.012
    Language: English
    Publisher: Elsevier BV
    Publication Date: 2004
    detail.hit.zdb_id: 2001948-8
    SSG: 12
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  • 8
    Online Resource
    Online Resource
    The Histone Variant H3.3 Marks Active Chromatin by Replication-Independent Nucleosome Assembly
    Elsevier BV ; 2002
    In:  Molecular Cell Vol. 9, No. 6 ( 2002-06), p. 1191-1200
    Details
    In: Molecular Cell, Elsevier BV, Vol. 9, No. 6 ( 2002-06), p. 1191-1200
    Type of Medium: Online Resource
    ISSN: 1097-2765
    URL: Article
    DOI: 10.1016/S1097-2765(02)00542-7
    Language: English
    Publisher: Elsevier BV
    Publication Date: 2002
    detail.hit.zdb_id: 2001948-8
    SSG: 12
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  • 9
    Online Resource
    Online Resource
    Histone H3 variants specify modes of chromatin assembly
    Proceedings of the National Academy of Sciences ; 2002
    In:  Proceedings of the National Academy of Sciences Vol. 99, No. suppl_4 ( 2002-12-10), p. 16477-16484
    Details
    In: Proceedings of the National Academy of Sciences, Proceedings of the National Academy of Sciences, Vol. 99, No. suppl_4 ( 2002-12-10), p. 16477-16484
    Abstract: Histone variants have been known for 30 years, but their functions and the mechanism of their deposition are still largely unknown. Drosophila has three versions of histone H3. H3 packages the bulk genome, H3.3 marks active chromatin and may be essential for gene regulation, and Cid is the characteristic structural component of centromeric chromatin. We have characterized the properties of these histones by using a Drosophila cell-line system that allows precise analysis of both DNA replication and histone deposition. The deposition of H3 is restricted to replicating DNA. In striking contrast, H3.3 and Cid deposit throughout the cell cycle. Deposition of H3.3 occurs without any corresponding DNA replication. To confirm that the deposition of Cid is also replication-independent (RI), we examined centromere replication in cultured cells and neuroblasts. We found that centromeres replicate out of phase with heterochromatin and display replication patterns that may limit H3 deposition. This confirms that both variants undergo RI deposition, but at different locations in the nucleus. How variant histones accomplish RI deposition is unknown, and raises basic questions about the stability of nucleosomes, the machinery that accomplishes nucleosome assembly, and the functional organization of the nucleus. The different in vivo properties of H3, H3.3, and Cid set the stage for identifying the mechanisms by which they are differentially targeted. Here we suggest that local effects of “open” chromatin and broader effects of nuclear organization help to guide the two different H3 variants to their target sites.
    Type of Medium: Online Resource
    ISSN: 0027-8424 , 1091-6490
    URL: Article
    DOI: 10.1073/pnas.172403699
    RVK:
    TA 1000
    RVK:
    WA 15000
    Language: English
    Publisher: Proceedings of the National Academy of Sciences
    Publication Date: 2002
    detail.hit.zdb_id: 209104-5
    detail.hit.zdb_id: 1461794-8
    SSG: 11
    SSG: 12
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  • 10
    Online Resource
    Online Resource
    Heterochromatic deposition of centromeric histone H3-like proteins
    Proceedings of the National Academy of Sciences ; 2000
    In:  Proceedings of the National Academy of Sciences Vol. 97, No. 2 ( 2000-01-18), p. 716-721
    Details
    In: Proceedings of the National Academy of Sciences, Proceedings of the National Academy of Sciences, Vol. 97, No. 2 ( 2000-01-18), p. 716-721
    Abstract: Centromeres of most organisms are embedded within constitutive heterochromatin, the condensed regions of chromosomes that account for a large fraction of complex genomes. The functional significance of this centromere–heterochromatin relationship, if any, is unknown. One possibility is that heterochromatin provides a suitable environment for assembly of centromere components, such as special centromeric nucleosomes that contain distinctive histone H3-like proteins. We describe a Drosophila H3-like protein, Cid (for centromere identifier) that localizes exclusively to fly centromeres. When the cid upstream region drives expression of H3 and H2B histone–green fluorescent protein fusion genes in Drosophila cells, euchromatin-specific deposition results. Remarkably, when the cid upstream region drives expression of yeast, worm, and human centromeric histone–green fluorescent protein fusion proteins, localization is preferentially within Drosophila pericentric heterochromatin. Heterochromatin-specific localization also was seen for yeast and worm centromeric proteins constitutively expressed in human cells. Preferential localization to heterochromatin in heterologous systems is unexpected if centromere-specific or site-specific factors determine H3-like protein localization to centromeres. Rather, the heterochromatic state itself may help localize centromeric components.
    Type of Medium: Online Resource
    ISSN: 0027-8424 , 1091-6490
    URL: Article
    DOI: 10.1073/pnas.97.2.716
    RVK:
    TA 1000
    RVK:
    WA 15000
    Language: English
    Publisher: Proceedings of the National Academy of Sciences
    Publication Date: 2000
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    detail.hit.zdb_id: 1461794-8
    SSG: 11
    SSG: 12
    Location Call Number Limitation Availability
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