Kanazawa University researchers observe DNA capture mechanism by Smc5/6 protein
Researchers used high-speed atomic force microscopy to observe how the Smc5/6 protein complex shifts shape to capture, tether, and compact DNA strands.
A research team from Kanazawa University and the National Institute of Genetics in Japan has visualized the mechanical interactions between the Smc5/6 protein assembly and DNA. By employing high-speed atomic force microscopy (HS-AFM), the researchers captured real-time structural transitions that occur as the protein interacts with genetic material.
The study identified two primary configurations of the Smc5/6 structure, which are influenced by the presence of adenosine triphosphate (ATP). The protein complex transitions between these states to grip DNA, pull separate strands together, and stabilize twisted arrangements. This process allows for more efficient compaction of DNA, a function vital for the maintenance and repair of chromosomes.
Lead researcher Kenichi Umeda noted that observing these individual structural changes clarifies how the protein carries out its biological roles. By visualizing the movement at the nanometer scale, the researchers were able to link specific shape shifts to the capture and tethering functions of the assembly.
While this study provides new insights into fundamental molecular biology, the researchers noted that the findings were derived from purified proteins in a laboratory setting. This foundation of basic research could eventually inform broader studies regarding chromosomal stability and DNA maintenance failures.