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Showing 1–11 of 11 results
Advanced filters: Author: Adam Ben-Shem Clear advanced filters

  • Eukaryotic ribosomal proteins contain nuclear localization signals (NLSs) that their bacterial counterparts lack. Here the authors compare homologous proteins from bacterial and eukaryotic ribosomes to show how NLSs could emerge in the course of evolution, and use this knowledge to identify novel NLSs.

    • Sergey Melnikov
    • Adam Ben-Shem
    • Marat Yusupov
    ResearchOpen Access
    Nature Communications
    Volume: 6, P: 1-5

  • The structure of human TIP60-C uncovers a molecular machine that modifies and exchanges histones in the nucleosome, illustrating how vertebrates merge these activities, which are carried out by two independent assemblies in yeast.

    • Changqing Li
    • Ekaterina Smirnova
    • Adam Ben-Shem
    ResearchOpen Access
    Nature
    Volume: 635, P: 764-769

  • Structural studies on the yeast transcription coactivator complex SAGA (Spt–Ada–Gcn5–acetyltransferase) provide insights into the mechanism of initiation of regulated transcription by this multiprotein complex, which is conserved among eukaryotes.

    • Gabor Papai
    • Alexandre Frechard
    • Adam Ben-Shem
    Research
    Nature
    Volume: 577, P: 711-716

  • Transcription preinitiation complex assembly begins with the recognition of the gene promoter by the TATA-box Binding Protein-containing TFIID complex. Here the authors present a Cryo-EM structure of promoter-bound yeast TFIID complex, providing a detailed view of its subunit organization and promoter DNA contacts.

    • Olga Kolesnikova
    • Adam Ben-Shem
    • Gabor Papai
    ResearchOpen Access
    Nature Communications
    Volume: 9, P: 1-10

  • The transcription co-activator complex SAGA is recruited to promoters by transcriptional activators and promotes the formation of the pre-initiation complex. Here, the authors present the cryo-EM structure of the SAGA complex and resolve the major target of activator binding, the 430 kDa Tra1 protein.

    • Grigory Sharov
    • Karine Voltz
    • Patrick Schultz
    ResearchOpen Access
    Nature Communications
    Volume: 8, P: 1-7

  • The recent X-ray structures of the complete ribosome and large and small subunits from eukaryotes allow these structures to be compared to the previously determined structures of bacterial ribosomes. This Review describes bacterial and eukaryotic ribosomes as a conserved core and two specific shells and focuses on selected bacteria- and eukaryote-specific structural features and their functional implications.

    • Sergey Melnikov
    • Adam Ben-Shem
    • Marat Yusupov
    Reviews
    Nature Structural & Molecular Biology
    Volume: 19, P: 560-567