7A8R

Structure of RecQL from Bos taurus

7A8R の概要

• エントリーDOI: 10.2210/pdb7a8r/pdb
• 分子名称: ATP-dependent DNA helicase, ZINC ION, ADENOSINE-5'-DIPHOSPHATE, ... (5 entities in total)
• 機能のキーワード: helicase, dna repair, holliday junction, recombination
• 由来する生物種: Bos taurus (Bovine)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 122144.49

構造登録者

Rety, S.,Chen, W.F.,Xi, X.G. (登録日: 2020-08-30, 公開日: 2021-10-06, 最終更新日: 2024-01-31)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.31 Å)