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Structure paper

TitleStructural insights into transcriptional regulation by the helicase RECQL5.
Journal, issue, pagesNat Struct Mol Biol, Vol. 32, Issue 9, Page 1721-1730, Year 2025
Publish dateJul 7, 2025
AuthorsAlfredo Jose Florez Ariza / Nicholas Z Lue / Patricia Grob / Benjamin Kaeser / Jie Fang / Susanne A Kassube / Eva Nogales /
PubMed AbstractTranscription poses a major challenge for genome stability. The RECQL5 helicase helps safeguard genome integrity and is the only member of the human RecQ helicase family that directly binds to RNA ...Transcription poses a major challenge for genome stability. The RECQL5 helicase helps safeguard genome integrity and is the only member of the human RecQ helicase family that directly binds to RNA polymerase II (Pol II) and affects its progression. While RECQL5 mitigates transcription stress in cells, the molecular mechanism underlying this phenomenon is unclear. Here, we use cryo-electron microscopy to determine the structures of stalled human Pol II elongation complexes (ECs) bound to RECQL5. Our structures reveal the molecular interactions stabilizing RECQL5 binding to the Pol II EC and highlight its role as a transcriptional roadblock. Additionally, we find that, in its nucleotide-free state, RECQL5 twists the downstream DNA in the EC and, upon nucleotide binding, undergoes a conformational change that allosterically induces Pol II toward a post-translocation state. We propose that this mechanism may help restart Pol II elongation and, therefore, contribute to reducing transcription stress.
External linksNat Struct Mol Biol / PubMed:40624164 / PubMed Central
MethodsEM (single particle)
Resolution2.6 - 3.7 Å
Structure data

48071

9ehz

EMDB-48071, PDB-9ehz:
Cryo-EM structure of Human RNA polymerase II Elongation Complex in an Intermediate Translocation State
Method: EM (single particle) / Resolution: 2.6 Å

48073

9ei1

EMDB-48073, PDB-9ei1:
Cryo-EM structure of Human RNA polymerase II Elongation Complex bound to the RECQL5 helicase in the absence of nucleotide
Method: EM (single particle) / Resolution: 3.2 Å

48074

9ei2

EMDB-48074, PDB-9ei2:
Cryo-EM structure of Human RNA polymerase II Elongation Complex bound to an apo RECQL5 helicase (RECQL5 IRI Module focused-classified)
Method: EM (single particle) / Resolution: 2.8 Å

48075

9ei3

EMDB-48075, PDB-9ei3:
Cryo-EM structure of Human RNA polymerase II Elongation Complex bound to the RECQL5 helicase in the presence of AMPPNP
Method: EM (single particle) / Resolution: 3.2 Å

48076

9ei4

EMDB-48076, PDB-9ei4:
Cryo-EM structure of Human RNA polymerase II Elongation Complex bound to the RECQL5 helicase in the presence of ADP
Method: EM (single particle) / Resolution: 3.7 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-MG:
Unknown entry

ChemComp-ANP:
PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER / AMP-PNP, energy-carrying molecule analogue*YM

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM

Source
  • homo sapiens (human)
KeywordsTRANSCRIPTION / TRANSFERASE/DNA/RNA / translocation / Human RNA polymerase II / TRANSFERASE-DNA-RNA complex / RECQL5 helicase / IRI Module

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