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  • American Association for the Advancement of Science (AAAS)  (5)
  • Springer Nature  (1)
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  • 1
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    American Association for the Advancement of Science (AAAS)
    In: Science
    Publikationsdatum: 2018
    Beschreibung: 〈p〉Genomic DNA forms chromatin, in which the nucleosome is the repeating unit. The mechanism by which RNA polymerase II (RNAPII) transcribes the nucleosomal DNA remains unclear. Here we report the cryo–electron microscopy structures of RNAPII-nucleosome complexes in which RNAPII pauses at the superhelical locations SHL(–6), SHL(–5), SHL(–2), and SHL(–1) of the nucleosome. RNAPII pauses at the major histone-DNA contact sites, and the nucleosome interactions with the RNAPII subunits stabilize the pause. These structures reveal snapshots of nucleosomal transcription, in which RNAPII gradually tears DNA from the histone surface while preserving the histone octamer. The nucleosomes in the SHL(–1) complexes are bound to a "foreign" DNA segment, which might explain the histone transfer mechanism. These results provide the foundations for understanding chromatin transcription and epigenetic regulation.〈/p〉
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
    BibTip Andere fanden auch interessant ...
  • 2
    Publikationsdatum: 2014-02-28
    Beschreibung: Nature Geoscience 7, 224 (2014). doi:10.1038/ngeo2074 Authors: M. Nishi, T. Irifune, J. Tsuchiya, Y. Tange, Y. Nishihara, K. Fujino & Y. Higo The presence of water strongly influences the structure, composition and dynamics of the Earth’s deep mantle. Hydrous magnesium-rich silicates play an important role in transporting water into the deep mantle when oceanic plates subduct as slabs. The highest-pressure form of such hydrous silicates, phase D, was reported to dissociate into an assemblage of nominally anhydrous phases plus water at pressures of about 44 GPa, equivalent to 1,250 km depth. In this way, free water would be released in the middle region of the lower mantle, which suggests that no water can reach the deeper regions of the lower mantle. Here we use in situ X-ray measurements in conjunction with a multi-anvil apparatus using sintered diamond anvils to show that hydrous phases are stable under lower mantle conditions up to 50 GPa. We found that phase D transforms to an assemblage with another hydrous silicate (MgSiH2O4), named phase H, at pressures above about 48 GPa. Our results suggest that phase H is the dominant hydrous silicate in descending slabs, and may be found at depths far deeper than 1,250 km. We conclude that a significant amount of water is retained in the descending slabs and may be delivered to the deepest part of the lower mantle.
    Print ISSN: 1752-0894
    Digitale ISSN: 1752-0908
    Thema: Geologie und Paläontologie
    Publiziert von Springer Nature
    Standort Signatur Erwartet Verfügbarkeit
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  • 3
    Publikationsdatum: 2019
    Beschreibung: 〈p〉RNA polymerase II (RNAPII) transcribes chromosomal DNA that contains multiple nucleosomes. The nucleosome forms transcriptional barriers, and nucleosomal transcription requires several additional factors in vivo. We demonstrate that the transcription elongation factors Elf1 and Spt4/5 cooperatively lower the barriers and increase the RNAPII processivity in the nucleosome. The cryo–electron microscopy structures of the nucleosome-transcribing RNAPII elongation complexes (ECs) reveal that Elf1 and Spt4/5 reshape the EC downstream edge and intervene between RNAPII and the nucleosome. They facilitate RNAPII progression through superhelical location SHL(–1) by adjusting the nucleosome in favor of the forward progression. They suppress pausing at SHL(–5) by preventing the stable RNAPII-nucleosome interaction. Thus, the EC overcomes the nucleosomal barriers while providing a platform for various chromatin functions.〈/p〉
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
    BibTip Andere fanden auch interessant ...
  • 4
    Publikationsdatum: 2019
    Beschreibung: 〈p〉RNA polymerase II (RNAPII) transcribes chromosomal DNA that contains multiple nucleosomes. The nucleosome forms transcriptional barriers, and nucleosomal transcription requires several additional factors in vivo. We demonstrate that the transcription elongation factors Elf1 and Spt4/5 cooperatively lower the barriers and increase the RNAPII processivity in the nucleosome. The cryo–electron microscopy structures of the nucleosome-transcribing RNAPII elongation complexes (ECs) reveal that Elf1 and Spt4/5 reshape the EC downstream edge and intervene between RNAPII and the nucleosome. They facilitate RNAPII progression through superhelical location SHL(–1) by adjusting the nucleosome in favor of the forward progression. They suppress pausing at SHL(–5) by preventing the stable RNAPII-nucleosome interaction. Thus, the EC overcomes the nucleosomal barriers while providing a platform for various chromatin functions.〈/p〉
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Allgemeine Naturwissenschaft
    Standort Signatur Erwartet Verfügbarkeit
    BibTip Andere fanden auch interessant ...
  • 5
    Publikationsdatum: 2018
    Beschreibung: 〈p〉Genomic DNA forms chromatin, in which the nucleosome is the repeating unit. The mechanism by which RNA polymerase II (RNAPII) transcribes the nucleosomal DNA remains unclear. Here we report the cryo–electron microscopy structures of RNAPII-nucleosome complexes, in which RNAPII pauses at the superhelical locations, SHL(-6), SHL(-5), SHL(-2), and SHL(-1), of the nucleosome. RNAPII pauses at the major histone-DNA contact sites, and the nucleosome interactions with the RNAPII subunits stabilize the pause. These structures reveal snapshots of nucleosomal transcription, where RNAPII gradually tears DNA from the histone surface, while preserving the histone octamer. Interestingly, the nucleosomes in the SHL(-1) complexes are bound to a "foreign" DNA segment, which might explain the histone transfer mechanism. These results provide the foundations for understanding chromatin transcription and epigenetic regulation.〈/p〉
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Allgemeine Naturwissenschaft
    Standort Signatur Erwartet Verfügbarkeit
    BibTip Andere fanden auch interessant ...
  • 6
    facet.materialart.
    Unbekannt
    American Association for the Advancement of Science (AAAS)
    In: Science
    Publikationsdatum: 2018-11-02
    Beschreibung: Genomic DNA forms chromatin, in which the nucleosome is the repeating unit. The mechanism by which RNA polymerase II (RNAPII) transcribes the nucleosomal DNA remains unclear. Here we report the cryo–electron microscopy structures of RNAPII-nucleosome complexes in which RNAPII pauses at the superhelical locations SHL(–6), SHL(–5), SHL(–2), and SHL(–1) of the nucleosome. RNAPII pauses at the major histone-DNA contact sites, and the nucleosome interactions with the RNAPII subunits stabilize the pause. These structures reveal snapshots of nucleosomal transcription, in which RNAPII gradually tears DNA from the histone surface while preserving the histone octamer. The nucleosomes in the SHL(–1) complexes are bound to a "foreign" DNA segment, which might explain the histone transfer mechanism. These results provide the foundations for understanding chromatin transcription and epigenetic regulation.
    Schlagwort(e): Biochemistry
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Geologie und Paläontologie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
    BibTip Andere fanden auch interessant ...
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