Watch how accessories are organized by ritual growth in actual time

Using optical tweezers, researchers at the National University of Taiwan noticed individual link events, providing new visions about the molecular regulation of identical repharience.

New Ticket Posted in Nuclear acid research It reveals how the subordinate proteins regulate the growth of Rad51 threads, which is a decisive step in the reset and DNA repair.

Research, led by Professor Hong Win Lee (Chemistry Department) and Professor Peter Che (Biochemical Sciences Institute), biomedic bridges and biochemistry to address one of the central challenges in DNA reform: how to assemble RAD51 on DNA in real time.

Traditional structural techniques capture only fixed or medium views of protein groups, leaving without answering any forms that drive the growth of ritual growth.

To overcome this, the team applied a mono visual tweezer, which uses concentrated laser beams to treat DNA molecules connected to microscopic beads. Since the Rad51 proteins are binding and extended along the DNA, the changes resulting from the length are tracked with a nanometer, allowing researchers to monitor the growth of the gradual threads directly.

This approach revealed an amazing organizational role for dependency proteins. Rad51 alone was assembled primarily in Octair units, but in the presence of the SWI5-SFR1 complex, the assembly turned into quadruple. These Rad51 threads settled, making the assembly more consistent and efficient.

These ideas shed light on how to re -install dependency proteins to adjust the genome safety. Besides our understanding of the DNA repair, the results carry effects on cancer biology and genome editing techniques.

“This work explains how one -molecular platform can illuminate, along with multidisciplinary cooperation, basic biological processes with unprecedented details,” says Professor Hong Win Lee.