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

News and Comment

  • News & Views |

    The CRISPR–Cas enzyme Cas9 faces the challenge of identifying a specific nucleotide sequence within double-stranded DNA. New cryo-EM and biochemical studies show that in the earliest steps of binding, Cas9 bends the DNA and promotes unwinding of two base pairs, enabling it to efficiently scan the sequence of this critical region.

    • Selma Sinan
    •  & Rick Russell
  • News & Views |

    A series of new cryo-EM structures reveals a surprising twist in how the RAG complex initiates V(D)J recombination. The initial complex with substrate DNA adopts two conformations: in one, the DNA is relatively undistorted but the scissile phosphate is far from the active site, and in the other the DNA is partially melted and unwound by half a turn, which allows the scissile phosphate to dock into the active site. Similar pre-catalysis DNA melting may occur with other DDE recombinases, for which equivalent complexes with uncleaved substrate DNA are not yet available.

    • Fred Dyda
    •  & Phoebe A. Rice
  • Research Highlights |

    DROSHA and its partner DGCR8 form a heterotrimeric complex named Microprocessor, which is essential for microRNA biogenesis. A recent study by Kwon et al. in Cell reveals the structure of a DROSHA construct in complex with the C-terminal region of DGCR8, thereby unveiling the topology and interactions between components of the Microprocessor and insights into its 'ruler'-based cleavage activity and function.

    • Sisi Li
    •  & Dinshaw J Patel
    Cell Research 26, 511-512