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TitleStructural mimicry in transcription regulation of human RNA polymerase II by the DNA helicase RECQL5.
Journal, issue, pagesNat Struct Mol Biol, Vol. 20, Issue 7, Page 892-899, Year 2013
Publish dateJun 9, 2013
AuthorsSusanne A Kassube / Martin Jinek / Jie Fang / Susan Tsutakawa / Eva Nogales /
PubMed AbstractRECQL5 is a member of the highly conserved RecQ family of DNA helicases involved in DNA repair. RECQL5 interacts with RNA polymerase II (Pol II) and inhibits transcription of protein-encoding genes ...RECQL5 is a member of the highly conserved RecQ family of DNA helicases involved in DNA repair. RECQL5 interacts with RNA polymerase II (Pol II) and inhibits transcription of protein-encoding genes by an unknown mechanism. We show that RECQL5 contacts the Rpb1 jaw domain of Pol II at a site that overlaps with the binding site for the transcription elongation factor TFIIS. Our cryo-EM structure of elongating Pol II arrested in complex with RECQL5 shows that the RECQL5 helicase domain is positioned to sterically block elongation. The crystal structure of the RECQL5 KIX domain reveals similarities with TFIIS, and binding of RECQL5 to Pol II interferes with the ability of TFIIS to promote transcriptional read-through in vitro. Together, our findings reveal a dual mode of transcriptional repression by RECQL5 that includes structural mimicry of the Pol II-TFIIS interaction.
External linksNat Struct Mol Biol / PubMed:23748380 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution1.9 - 13.0 Å
Structure data

EMDB-2367:
Structural mimicry in transcription regulation of human RNA polymerase II by the DNA helicase RECQL5
Method: EM (single particle) / Resolution: 13.0 Å

PDB-4bk0:
Crystal structure of the KIX domain of human RECQL5 (domain-swapped dimer)
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

Chemicals

ChemComp-PEG:
DI(HYDROXYETHYL)ETHER

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
  • unidentified (others)
KeywordsTRANSCRIPTION / DNA HELICASE / TRANSCRIPTIONAL REPRESSION

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