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Showing 1–14 of 14 results
Advanced filters: Author: Meindert H Lamers Clear advanced filters

  • Sarah Fortune, Meindert Lamers and colleagues show that, unlike Escherichia coli, Mycobacterium tuberculosis uses an exonuclease domain in polymerase DnaE1 to proofread DNA replication. Importantly, this proofreading mechanism renders mycobacteria sensitive to nucleoside analogs, a class of small molecules used to treat viral infections and cancer.

    • Jeremy M Rock
    • Ulla F Lang
    • Meindert H Lamers
    Research
    Nature Genetics
    Volume: 47, P: 677-681

  • Cryo–EM reconstructions and atomic models reveal the mechanism of MutS–MutL DNA mismatch recognition and repair initiation.

    • Rafael Fernandez-Leiro
    • Doreth Bhairosing-Kok
    • Meindert H. Lamers
    Research
    Nature Structural & Molecular Biology
    Volume: 28, P: 373-381

  • Cryogenic electron microscopy structures of Escherichia coli MutS at sequential stages of the ATP hydrolysis cycle reveal how ATP binding and hydrolysis and its modulation by DNA enable MutS to adopt different conformations during mismatch repair.

    • Alessandro Borsellini
    • Vladislav Kunetsky
    • Meindert H. Lamers
    Research
    Nature Structural & Molecular Biology
    Volume: 29, P: 59-66

  • Here, using structural and biochemical data, the authors provide a comprehensive overview of Okazaki fragment maturation in Escherichia coli, demonstrating a relay of events among the involved enzymes regulating an efficient four-point molecular handover.

    • Margherita M. Botto
    • Alessandro Borsellini
    • Meindert H. Lamers
    Research
    Nature Structural & Molecular Biology
    Volume: 30, P: 1505-1515

  • Single-stranded DNA-binding proteins protect exposed DNA during replication but create potential barriers for polymerases. Here, the authors reveal that DNA polymerase actively and sequentially displaces stationary SSB proteins. The SSB C-terminal tail facilitates this process by reducing energy barriers for displacement to ensure DNA replication.

    • Longfu Xu
    • Shikai Jin
    • Gijs J. L. Wuite
    ResearchOpen Access
    Nature Communications
    Volume: 16, P: 1-16

  • Ethylene glycol is a monomer of the ubiquitous plastic polyethylene terephthalate (PET). Here, the authors report the discovery of NAD-dependent alcohol and aldehyde dehydrogenases in the soil bacterium Paracoccus denitrificans for ethylene glycol catabolism.

    • Minrui Ren
    • Danni Li
    • Lennart Schada von Borzyskowski
    ResearchOpen Access
    Nature Communications
    Volume: 16, P: 1-15

  • In high fidelity DNA polymerases the exonuclease site is distal from the polymerization site and it is unknown how the primer strand travels between the two sites when mis-incorporated nucleotides must be removed. Here, the authors perform MD simulations and identify an optimal path for DNA primer strand translocation in the E. coli replicative DNA polymerase III and characterise the kinetics and dynamics of the Pol III pol-to-exo mode transition, which is validated with mutagenesis experiments.

    • Thomas Dodd
    • Margherita Botto
    • Ivaylo Ivanov
    ResearchOpen Access
    Nature Communications
    Volume: 11, P: 1-11

  • Classical non-homologous end-joining (cNHEJ) is the dominant pathway used by human cells to repair DNA double-strand breaks (DSBs) and maintain genome stability. Here the authors show that PARP1-driven chromatin expansion allows the recruitment of ZNF384, which in turn recruits Ku70/Ku80 to facilitate cNHEJ.

    • Jenny Kaur Singh
    • Rebecca Smith
    • Haico van Attikum
    ResearchOpen Access
    Nature Communications
    Volume: 12, P: 1-21

  • Cryo-EM and NMR analyses of the E. coli replisome show how DNA-end fraying after mismatch incorporation at the polymerase active site enables substrate ends to reach the ‘proofreading’ exonuclease site for mismatch removal.

    • Rafael Fernandez-Leiro
    • Julian Conrad
    • Meindert H Lamers
    Research
    Nature Structural & Molecular Biology
    Volume: 24, P: 140-143

  • The polymerase and histidinol phosphatase (PHP) domain in the DNA polymerase DnaE1 is essential for mycobacterial high-fidelity DNA replication. Here, the authors determine the DnaE1 crystal structure, which reveals the PHP-exonuclease mechanism that can be exploited for antibiotic development.

    • Soledad Baños-Mateos
    • Anne-Marie M. van Roon
    • Meindert H. Lamers
    ResearchOpen Access
    Nature Communications
    Volume: 8, P: 1-10

  • The AMR Accelerator is an Innovative Medicines Initiative programme integrating nine projects with the shared goal of progressing the development of new antibiotics and building antimicrobial resistance research capability. Five years in, we reflect on the programme’s value, results and key challenge: ensuring the sustainability of assets, infrastructures and expertise.

    • Josepine Fernow
    • Marie Olliver
    • Anders Karlén
    Comments & Opinion
    Nature Reviews Drug Discovery
    Volume: 24, P: 1-2