Publications by authors named "Ako Kagawa"
Article Synopsis
- The study highlights the significance of enzyme assembly states in regulating enzyme function, particularly focusing on L-lactate oxidase (LOX) and its interaction with poly-L-lysine (PLL).
- In the presence of ammonium sulfate, LOX forms larger micrometer-scale droplets that enhance its enzyme activity significantly compared to its dispersed form.
- The findings suggest that the changes in LOX conformation in assemblies lead to increased activation, offering insights into enzyme behavior in living cells and potential biotechnological applications.
Rad52 plays essential roles in homology-dependent double-strand break repair. Various studies have established the functions of Rad52 in Rad51-dependent and Rad51-independent repair processes. However, the precise molecular mechanisms of Rad52 in these processes remain unknown.
View Article and Find Full Text PDFThe process of homologous recombination is indispensable for both meiotic and mitotic cell division, and is one of the major pathways for double-strand break (DSB) repair. The human Rad54B protein, which belongs to the SWI2/SNF2 protein family, plays a role in homologous recombination, and may function with the Dmc1 recombinase, a meiosis-specific Rad51 homolog. In the present study, we found that Rad54B enhanced the DNA strand-exchange activity of Dmc1 by stabilizing the Dmc1-single-stranded DNA (ssDNA) complex.
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