7A8R

Structure of RecQL from Bos taurus

Summary for 7A8R

• Entry DOI: 10.2210/pdb7a8r/pdb
• Descriptor: ATP-dependent DNA helicase, ZINC ION, ADENOSINE-5'-DIPHOSPHATE, ... (5 entities in total)
• Functional Keywords: helicase, dna repair, holliday junction, recombination
• Biological source: Bos taurus (Bovine)
• Total number of polymer chains: 2
• Total formula weight: 122144.49

Authors

Rety, S.,Chen, W.F.,Xi, X.G. (deposition date: 2020-08-30, release date: 2021-10-06, Last modification date: 2024-01-31)

Primary citation

Liu, N.N.,Song, Z.Y.,Guo, H.L.,Yin, H.,Chen, W.F.,Dai, Y.X.,Xin, B.G.,Ai, X.,Ji, L.,Wang, Q.M.,Hou, X.M.,Dou, S.X.,Rety, S.,Xi, X.G.
Endogenous Bos taurus RECQL is predominantly monomeric and more active than oligomers.
Cell Rep, 36:109688-109688, 2021

PubMed Abstract: There is broad consensus that RecQ family helicase is a high-order oligomer that dissociates into a dimer upon ATP binding. This conclusion is based mainly on studies of highly purified recombinant proteins, and the oligomeric states of RecQ helicases in living cells remain unknown. We show here that, in contrast to current models, monomeric RECQL helicase is more abundant than oligomer/dimer forms in living cells. Further characterization of endogenous BtRECQL and isolated monomeric BtRECQL using various approaches demonstrates that both endogenous 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 as efficiently as human RECQL and BLM helicases. These discoveries have implications for understanding endogenous RECQL oligomeric structures and their regulation. It is worth revisiting oligomeric states of the other members of the RecQ family helicases in living cells.

PubMed: 34496242
DOI: 10.1016/j.celrep.2021.109688

Experimental method

X-RAY DIFFRACTION (2.31 Å)