The discovery of non-canonical telomeric dsDNA-binding proteins in Caenorhabditis elegans reveal their contribution in the maintenance of telomere length and germline immortality.
X-ray crystallography reveals that the Dna2 nuclease-helicase contains a long tunnel through which single-stranded DNA threads, and an allosteric mechanism for displacing the DNA-binding protein Rpa that restricts cleavage to the proper polarity.
Single-molecule force and fluorescence spectroscopy reveal the structural states and dynamics of E. coli single-stranded DNA binding proteins and the energy landscape of the nucleo–protein complex.
The structure of phage L's Dec demonstrates a new fold within this family of proteins, and shows modulation of capsid binding occurs through two sites, with site 1 being preferred.
Biochemical reconstitution experiments uncover the ubiquitin-mediated function of a DNA repair protein, key to the understanding of Fanconi Anemia, a cancer-associated bone marrow failure syndrome.
hRPA permits the BLM helicase to bidirectionally unwind DNA from a nick which could potentially facilitate its function switching in DNA repair and promote end resection in homologous recombination.
RecO efficiently displaces SSB from ssDNA without consuming ATPs using its two DNA-binding sites, even though SSB binds to ssDNA approximately 300 times more strongly than RecO does.
The crystal structure of Pur-alpha in complex with DNA reveals its molecular mechanisms of nucleic-acid binding and unwinding, allowing for a better understanding of its essential role in neurons.
