Nucleases are hydrolytic enzymes (hydrolases) that cleave the phosphodiester bond between nucleotides within nucleic acids, either within the nucleic acid chain (as in endonucleases) or from the end of the chain (as in exonucleases).

Latest Research and Reviews

  • Research | | open

    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
    • , Yuno Lee
    • , Suyeon Park
    • , Phuong Lien Hoang
    • , HyeokJin Cho
    • , Jeongmin Yu
    • , Thi Minh Hoa Vo
    • , Minsang Shin
    • , Mi Sun Jin
    • , Daeho Park
    • , Changbong Hyeon
    •  & Gwangrog Lee
  • Reviews |

    RNA is controlled at various stages of transcription and processing to achieve appropriate gene regulation. Whereas much research has focused on the cytoplasmic control of RNA levels, this Review discusses our emerging appreciation of the importance of nuclear RNA regulation, including the molecular machinery involved in nuclear RNA decay, how functional RNAs bypass degradation and roles for nuclear RNA decay in physiology and disease.

    • Manfred Schmid
    •  & Torben Heick Jensen
  • Research | | open

    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
    • , Elleke F. Bosma
    • , Valentijn Vrouwe
    • , Max Finger Bou
    • , Mihris I. S. Naduthodi
    • , Alex Gussak
    • , Rudolf B. L. Brinkman
    • , Richard van Kranenburg
    •  & John van der Oost
  • Research | | open

    CRISPR RNA-guided endonuclease Cas9 recognizes and cleaves the double-stranded DNA complementary to the RNA guide. Here the authors use high-speed atomic force micropcopy (HS-AFM) to visualize the conformational dynamics of Cas9 during its DNA targeting and cleavage processes.

    • Mikihiro Shibata
    • , Hiroshi Nishimasu
    • , Noriyuki Kodera
    • , Seiichi Hirano
    • , Toshio Ando
    • , Takayuki Uchihashi
    •  & Osamu Nureki
  • Research | | open

    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
    • , Antonio Ariza
    • , Christopher J. Carnie
    •  & Dragana Ahel

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