Nucleases articles within Nature Communications

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  • Article
    | Open Access

    The Mre11-Rad50 (MR) complex has key functions in the detection, signaling and repair of DNA breaks. Here the authors use transmission electron microscopy to show MR oligomerization is governed by a small beta-sheet protruding from the head domain of Rad50 at the base of the MR structure, and reveal MR head domain oligomerization is required for efficient DNA end resection.

    • Vera M. Kissling
    • , Giordano Reginato
    •  & Matthias Peter

  • Article
    | Open Access

    New approaches to plant disease control are important for pathogens that are difficult to control by existing methods. Here, the authors report a potential strategy to combat plant viruses by cytosolic expressed protein-only RNase P and show its ability for in vitro cleavage of tRNA-like structures existing in many plant viruses.

    • Anthony Gobert
    • , Yifat Quan
    •  & Philippe Giegé

  • Article
    | Open Access

    Type III CRISPR-Cas systems are able to target transcriptionally active DNA sequences in phages and plasmids. Here, the authors reveal the mechanism of the target nucleic acid preference of Type III-A CRISPR-Cas complexes at the transcription bubble by a combination of structural and biochemical approaches.

    • Tina Y. Liu
    • , Jun-Jie Liu
    •  & Jennifer A. Doudna

  • Article
    | Open Access

    Metal ions at the active site of an enzyme act as cofactors and their dynamic fluctuations might influence enzyme activity. Here authors use single-molecule FRET to study λ-exonuclease and find that metal-ion-coordination is correlated with enzymatic reaction-steps.

    • Wonseok Hwang
    • , Jungmin Yoo
    •  & Gwangrog Lee

  • Article
    | Open Access

    CRISPR-Cas9 genome engineering tools have found wide application in a range of species, however they are unsuitable for applications at elevated temperatures. Here the authors characterise ThermoCas9 from which is functional from 20°C to 70°C.

    • Ioannis Mougiakos
    • , Prarthana Mohanraju
    •  & John van der Oost

  • Article
    | Open Access

    ZRANB3 (Zinc-finger, RAN-Binding domain containing 3) is a structure-specific endonuclease that is recruited to DNA breaks and stressed replication forks. Here the authors present the crystal structure of the ZRANB3 endonuclease domain and analyse how ZRANB3 is regulated by the DNA clamp PCNA.

    • Marek Sebesta
    • , Christopher D. O. Cooper
    •  & Dragana Ahel

  • Article
    | Open Access

    Nucleosome positioning and chromatin accessibility are important contributors to the regulation of gene expression. Here the authors describe a method that allows the simultaneous measurement of nucleosome occupancy and chromatin accessibility in the same assay, revealing new features of chromatin organization linked to gene regulation.

    • Jakub Mieczkowski
    • , April Cook
    •  & Michael Y. Tolstorukov

  • Article |

    FAN1 is a structure-specific nuclease that plays a major role in eliminating highly cytotoxic interstrand DNA crosslinks. Here, Zhao et al. present several crystal structures of FAN1 in complex with DNA substrates and biochemical analyses that establish how FAN1 functions to resolve interstrand DNA crosslinks.

    • Qi Zhao
    • , Xiaoyu Xue
    •  & Yong Xiong

  • Article
    | Open Access

    Bacterial endonuclease V enzymes are characterized as DNA repair proteins. Here the authors show that human endonuclease V is an inosine-specific ribonuclease, indicating a role for this enzyme in normal RNA metabolism rather than DNA repair.

    • Erik Sebastian Vik
    • , Meh Sameen Nawaz
    •  & Ingrun Alseth

  • Article
    | Open Access

    In Escherichia coli, the highly conserved enzyme endonuclease V has a role in DNA repair. Here the authors show that human endonuclease V is an inosine 3' endoribonuclease and that Tudor Staphylococcal nuclease enhances this activity, suggesting a role for human endonuclease V in RNA metabolism.

    • Yoko Morita
    • , Toshihiro Shibutani
    •  & Isao Kuraoka

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