Efficient coordination between the winged helix domain and the aromatic-rich loop restructures the ATPase domain and facilitates DNA unwinding by human RECQ1.

ABSTRACT: RecQ helicases can unwind a wide spectrum of DNA structures and thereby protect the cells from genome instability. Unwinding mechanisms have been extensively studied for bacterial and human RecQ helicases. DNA-induced winged helix (WH) domain repositioning and allosteric remodeling of the ATPase domain have been shown to be important for unwinding activity of bacterial RecQ helicases. In contrast, no such altered conformational state was observed for human RECQ1 upon DNA or nucleotide binding. In this study, we have crystallized and characterized an engineered RECQ1 containing a flexible glycine serine-rich linker inserted between the zinc binding and WH domains. The linker containing construct exhibits more efficient DNA binding and unwinding activity. A crystal structure of the engineere

SUBMITTER: Das T 

PROVIDER: S-EPMC12164578 | biostudies-literature | 2025 Jun

REPOSITORIES: biostudies-literature