Endogenous Bos taurus RECQL is predominantly monomeric and more active than oligomers.
Cell Rep, 36(10):109688.
There is broad consensus that RecQ family helicase is a high-order oligomer thatdissociates into a dimer upon ATP binding. This conclusion is based mainly onstudies of highly purified recombinant proteins, and the oligomeric states ofRecQ helicases in living cells remain unknown. We show here that, in contrast tocurrent models, monomeric RECQL helicase is more abundant than oligomer/dimerforms in living cells. Further characterization of endogenous BtRECQL andisolated monomeric BtRECQL using various approaches demonstrates that bothendogenous and recombinant monomeric BtRECQL effectively function as monomers,displaying higher helicase and ATPase activities than dimers and oligomers.Furthermore, monomeric BtRECQL unfolds intramolecular G-quadruplex DNA asefficiently as human RECQL and BLM helicases. These discoveries have implicationsfor understanding endogenous RECQL oligomeric structures and their regulation. Itis worth revisiting oligomeric states of the other members of the RecQ familyhelicases in living cells.
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