Qiuye Bao

TL;DR: A platform for in situ and real-time measurement of protein-induced conformational changes in dsDNA is presented and the effects of probe surface density on binding/bending kinetics are investigated.

TL;DR: The design, characterization and application of a single polypeptide chain IHF, termed scIHF2, which is used as a novel regulatory cofactor for recombination or other DNA transactions in mammalian cells that require or benefit from sequence-specific high precision DNA bending.

TL;DR: It is shown that this conformational switch can be employed to control the efficiency of site-specific recombination catalyzed by lambda integrase and holds potential for the design of metal-mediated switches for the investigation of functional relationships.

TL;DR: The Integrase (Int) site-specific recombinase of coliphage HK022 catalyzes integrative and excisive DNA recombination between two attachment (att) sites in human cells without the need to supply the accessory proteins Integration Host Factor (IHF) and Excisionase (Xis) as discussed by the authors.

TL;DR: It is reported that proper development of Utf1 null embryos almost entirely depends on the presence of functional Utf2 alleles in the parental germline, indicating that Utf 1’s proposed epigenetic role in ESC pluripotency in vitro may be linked to intergenerational epigenetic inheritance in vivo.