Supramolecular assembly articles within Nature

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  • Article
    | Open Access

    A method that uses a combination of optical trapping, fluorescence microscopy and microfluidics to analyse the internal structure of chromosomes shows that there is a distinct nonlinear stiffening of the chromosome in response to tension.

    • Anna E. C. Meijering
    • , Kata Sarlós
    •  & Gijs J. L. Wuite

  • Article |

    The cryo-electron microscopy structure of the yeast SWI/SNF complex bound to a nucleosome substrate provides insights into the chromatin-remodelling function of this family of protein complexes and suggests mechanisms by which the mutated proteins may cause cancer.

    • Yan Han
    • , Alexis A Reyes
    •  & Yuan He

  • Letter |

    The cryo-electron microscopy structure of the ten-subunit human transcription factor IIH, revealing the molecular architecture of the TFIIH core complex, the detailed structures of its constituent XPB and XPD ATPases, and how the core and kinase subcomplexes of TFIIH are connected.

    • Basil J. Greber
    • , Thi Hoang Duong Nguyen
    •  & Eva Nogales

  • Article |

    Cryo-electron microscopy structural models of the human pre-initiation complex at all major steps of transcription initiation at near atomic-level resolution are presented, providing new mechanistic insights into the processes of promoter melting and transcription-bubble formation, as well as an almost complete proposed structural model of all of the pre-initiation complex components and their interactions with DNA.

    • Yuan He
    • , Chunli Yan
    •  & Eva Nogales

  • Article |

    The cryo-electron microscopy structures of yeast initiation complexes containing the transcription factors TBP, TFIIA, TFIIB, TFIIE, and TFIIF and containing either closed or open promoter DNA are reported, providing mechanistic insights into DNA opening and template-strand loading.

    • C. Plaschka
    • , M. Hantsche
    •  & P. Cramer

  • Letter |

    This study shows how the yeast Ctf4 protein couples the DNA helicase, Cdc45–MCM–GINS, to DNA polymerase α — the GINS subunit of the helicase and the polymerase use a similar interaction to bind Ctf4, suggesting that, as Ctf4 is a trimer, two polymerases could be simultaneously coupled to a single helicase during lagging-strand synthesis.

    • Aline C. Simon
    • , Jin C. Zhou
    •  & Luca Pellegrini

  • Letter |

    The co-crystal structure of the T-box tRNA-binding region, stem I, bound to tRNA is solved, showing that this region not only binds the anticodon, but also cradles the entire tRNA, forming an extended interface; the two T-loop motifs of stem I mediate interactions similar to those of RNase P and the large ribosomal subunit, even though the three species do not share a common evolutionary ancestor.

    • Jinwei Zhang
    •  & Adrian R. Ferré-D’Amaré

  • Article |

    The APC/C is a large multiprotein complex that functions as an E3 ubiquitin ligase to regulate the cell cycle. Here, the entire APC/C complex is reconstituted, and in combination with structural studies a pseudo-atomic model for 70% of the complex is provided. These results contribute towards a molecular understanding of the roles of individual subunits in APC/C assembly and their interactions with co-activators, substrates and regulatory proteins.

    • Anne Schreiber
    • , Florian Stengel
    •  & David Barford

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