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TitleStructure of human lymphoid-specific helicase HELLS in its autoinhibited state.
Journal, issue, pagesNucleic Acids Res, Vol. 54, Issue 6, Year 2026
Publish dateMar 19, 2026
AuthorsGundeep Kaur / Ren Ren / Jisun Lee / John R Horton / Xing Zhang / Yang Gao / Taiping Chen / Xiaodong Cheng /
PubMed AbstractHelicase, Lymphoid Specific (HELLS), also known as Lymphoid-Specific Helicase (LSH), is a member of the SNF2 chromatin-remodeling family that regulates DNA methylation and heterochromatin ...Helicase, Lymphoid Specific (HELLS), also known as Lymphoid-Specific Helicase (LSH), is a member of the SNF2 chromatin-remodeling family that regulates DNA methylation and heterochromatin organization. Unlike most chromatin remodelers, HELLS is catalytically inactive in its apo form and requires the DNA-binding protein CDCA7 for activation, though the underlying mechanism has remained unclear. Here, we combine biochemical, biophysical, and cryo-electron microscopy analyses to define the structural basis of HELLS autoinhibition. HELLS alone assembles into a hexameric (trimer of dimers) architecture stabilized by interactions between its N-terminal coiled-coil (CC) domain and ATPase Lobe-1, while ATPase Lobe-2 remains flexible and disengaged. The CC domain functions both as an oligomerization scaffold and as an autoinhibitory module that restricts catalytic activity. Binding of CDCA7 and DNA promotes formation of an active HELLS-CDCA7-DNA ternary complex. CDCA7 recognizes hemimethylated CpG dinucleotides in both B-form and non-B-form DNA and stimulates HELLS ATPase activity. Together, these findings reveal the mechanism of HELLS autoinhibition and its activation by CDCA7 and DNA, providing new insight into how the HELLS-CDCA7-DNA ternary complex maintains DNA methylation and heterochromatin integrity.
External linksNucleic Acids Res / PubMed:41954988 / PubMed Central
MethodsEM (single particle)
Resolution2.86 - 5.76 Å
Structure data

73693

9z04

EMDB-73693, PDB-9z04:
Structure of human lymphoid-specific helicase HELLS in its auto-inhibitory state
Method: EM (single particle) / Resolution: 2.99 Å

73694

9z05

EMDB-73694: Structure of human lymphoid-specific helicase HELLS in its auto-inhibitory state
PDB-9z05: Structure of human lymphoid-specific helicase HELLS in its auto-inhibitory state (D3)
Method: EM (single particle) / Resolution: 2.86 Å

73695

9z06

EMDB-73695, PDB-9z06:
Structure of human lymphoid-specific helicase HELLS in its auto-inhibitory state
Method: EM (single particle) / Resolution: 3.39 Å

EMDB-73696: Structure of human lymphoid-specific helicase HELLS in its auto-inhibitory state
Method: EM (single particle) / Resolution: 3.47 Å

EMDB-73697: Focussed refinement map of ATPase lobe 2 of human lymphoid-specific helicase HELLS
Method: EM (single particle) / Resolution: 5.76 Å

Source
  • homo sapiens (human)
KeywordsDNA BINDING PROTEIN / lymphoid-specific helicase / SF2 chromatin remodeler / ICF syndrome / ATP-binding / Chromatin-binding

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