Hydrolases articles within Nature

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  • Article
    | Open Access

    We find that bile salt hydrolase N-acyltransferase activity can form bacterial bile acid amidates that are positively correlated with the colonization of gut bacteria that assist in the regulation of the bile acid metabolic network.

    • Bipin Rimal
    • , Stephanie L. Collins
    •  & Andrew D. Patterson

  • Article |

    A structural analysis focusing on plant immunity reveals how LRR-containing receptor-like proteins recognize pathogenic ligands and consequently become activated, with the data suggesting that these proteins target pathogens through two different mechanisms.

    • Yue Sun
    • , Yan Wang
    •  & Jijie Chai

  • Article
    | Open Access

    Through structural analysis of the activation of bacterial STING, the molecular basis of STING filament formation and TIR effector domain activation in antiphage signalling is defined.

    • Benjamin R. Morehouse
    • , Matthew C. J. Yip
    •  & Philip J. Kranzusch

  • Article
    | Open Access

    A study using a biochemical screen of 57 phages in two bacterial species identifies and characterizes proteins enabling phages to evade CBASS and Pycsar immune systems, and describes the mechanisms involved.

    • Samuel J. Hobbs
    • , Tanita Wein
    •  & Philip J. Kranzusch

  • Article |

    A bacterial enzyme is characterized and demonstrated to have Ni2+-dependent activity and high specificity for free guanidine enabling the bacteria to use guanidine as the sole nitrogen source for growth.

    • D. Funck
    • , M. Sinn
    •  & J. S. Hartig

  • Letter |

    A hydrolytic enzyme with a non-canonical organocatalytic mechanism was generated by introducing Nδ-methylhistidine into a designed active site using engineered translation components, allowing optimization of enzyme performance using laboratory evolution.

    • Ashleigh J. Burke
    • , Sarah L. Lovelock
    •  & Anthony P. Green

  • Letter |

    The sirtuin family of enzymes are known as NAD-dependent deacetylases, although some of them have very weak deacetylase activity; here human SIRT6, an enzyme important for DNA repair and transcription, is shown to remove long-chain fatty acyl groups from protein lysine residues, and to have a function in promoting tumour necrosis factor alpha secretion.

    • Hong Jiang
    • , Saba Khan
    •  & Hening Lin

  • Article |

    The small GTPase Rab5 has been proposed to be a master regulator of endosome biogenesis; using in vivo RNA interference and mathematical modelling it is shown here that the endolysosomal system is resilient to loss of Rab5 until its concentration drops below a critical level, at which point endosomes are lost, leading to increased serum low-density lipoprotein levels, alterations in metabolism and hepatocellular polarity.

    • Anja Zeigerer
    • , Jerome Gilleron
    •  & Marino Zerial

  • News & Views |

    Caspase-1 is one of the main culprits behind sepsis, a form of systemic inflammation. The related enzyme caspase-11 is also involved, but the relative roles of the two proteins have been confusing, until now. See Letter p.117

    • Douglas R. Green

  • Letter |

    The enzyme inositol polyphosphate phosphatase 4A (INPP4A) removes phosphate groups from phosphatidylinositol-3,4-bisphosphate, a key cellular lipid. Here, a crucial role for INPP4A in maintaining the integrity of the brain is described. Mice that lack this enzyme suffer from neurodegeneration in the striatum of the brain, as well as severe involuntary movements. When present, INPP4A protects neurons from a particular type of cell death.

    • Junko Sasaki
    • , Satoshi Kofuji
    •  & Takehiko Sasaki

  • Letter |

    Polycomb group (PcG) proteins are transcriptional repressors that modify chromatin and regulate important developmental genes. One PcG-associated, chromatin-modifying activity is an enzyme that ubiquitinates histone H2A of chromatin. Here, a fruitfly PcG complex that is associated with H2A deubiquitination, and thereby with gene repression, is identified. PcG-mediated gene silencing might thus involve a dynamic balance between ubiquitination and deubiquitination of H2A.

    • Johanna C. Scheuermann
    • , Andrés Gaytán de Ayala Alonso
    •  & Jürg Müller

  • Article |

    Dynamin is a protein that catalyses the fission of clathrin-coated endocytic vesicles from cellular membranes. To carry out fission, it must hydrolyse GTP. The mechanism by which it does so is unknown, although it does require dynamin's GTPase effector domain (GED). Here, the structure of a minimal GTPase–GED fusion protein constructed from human dynamin 1 is presented. The structure reveals the catalytic machinery and provides new insight into the mechanisms underlying dynamin-catalysed membrane fission.

    • Joshua S. Chappie
    • , Sharmistha Acharya
    •  & Fred Dyda

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