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Structure paper

TitleStructure and function of IWS1 in transcription elongation.
Journal, issue, pagesNucleic Acids Res, Vol. 54, Issue 9, Year 2026
Publish dateMay 5, 2026
AuthorsDella Syau / Felix Steinruecke / Sophie Roth / Ernst Schmid / Karen Adelman / Johannes C Walter / Lucas Farnung /
PubMed AbstractTranscription elongation by RNA polymerase II is a tightly regulated process that requires coordinated interactions between transcription elongation factors. IWS1 (Interacts with SPT6) has been ...Transcription elongation by RNA polymerase II is a tightly regulated process that requires coordinated interactions between transcription elongation factors. IWS1 (Interacts with SPT6) has been implicated as a core elongation factor, but its molecular role remains unclear. We show that the intrinsically disordered C-terminal region of IWS1 contains short linear motifs (SLiMs) that multivalently engage the elongation machinery. Using cryo-electron microscopy, we map SLiMs in IWS1 that interact with Pol II subunits RPB1, RPB2, and RPB5, as well as elongation factors DSIF, SPT6, and ELOF1. Functional assays demonstrate that distinct IWS1 SLiMs specify IWS1 recruitment and IWS1-dependent transcription stimulation. IWS1 recruitment to the transcription elongation complex depends on association via the RPB1 jaw and binding of downstream DNA. Transcription elongation stimulation requires interactions with the RPB2 lobe and ELOF1. We identify other transcription elongation factors including ELOA and RECQL5 that bind the RPB1 jaw and demonstrate that IWS1 protects the activated transcription elongation complex from RECQL5 inhibition. We also reveal the binding of the histone reader and IWS1 interactor LEDGF to a transcribed downstream nucleosome. Our findings establish IWS1 as a modular scaffold that helps organize the transcription elongation complex, illustrating how disordered regions regulate transcription elongation.
External linksNucleic Acids Res / PubMed:42134803 / PubMed Central
MethodsEM (single particle)
Resolution2.4 - 4.3 Å
Structure data

48353

9mlc

EMDB-48353, PDB-9mlc:
Pol II-DSIF-SPT6-PAF1c-TFIIS-IWS1-ELOF1-LEDGF-nucleosome activated elongation complex Composite map T
Method: EM (single particle) / Resolution: 2.4 Å

EMDB-48354: Pol II-DSIF-SPT6-PAF1c-TFIIS-IWS1-ELOF1-LEDGF-nucleosome activated elongation complex consensus map A
Method: EM (single particle) / Resolution: 2.4 Å

EMDB-48355: Pol II-DSIF-SPT6-PAF1c-TFIIS-IWS1-ELOF1-LEDGF-nucleosome IWS1+ELOF1 local map B
Method: EM (single particle) / Resolution: 2.6 Å

EMDB-48356: Pol II-DSIF-SPT6-PAF1c-TFIIS-IWS1-ELOF1-LEDGF-nucleosome IWS1 C-terminus local map C
Method: EM (single particle) / Resolution: 2.4 Å

EMDB-48357: Pol II-DSIF-SPT6-PAF1c-TFIIS-IWS1-ELOF1-LEDGF-nucleosome TFIIS local map D
Method: EM (single particle) / Resolution: 4.3 Å

EMDB-48358: Pol II-DSIF-SPT6-PAF1c-TFIIS-IWS1-ELOF1-LEDGF-nucleosome DSIF local map E
Method: EM (single particle) / Resolution: 2.7 Å

EMDB-48359: Pol II-DSIF-SPT6-PAF1c-TFIIS-IWS1-ELOF1-LEDGF-nucleosome RTF1 local map F
Method: EM (single particle) / Resolution: 2.8 Å

EMDB-48360: Pol II-DSIF-SPT6-PAF1c-TFIIS-IWS1-ELOF1-LEDGF-nucleosome 10-subunit Pol II local map G
Method: EM (single particle) / Resolution: 2.5 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-MG:
Unknown entry

Source
  • homo sapiens (human)
  • sus scrofa (pig)
  • synthetic construct (others)
  • xenopus laevis (African clawed frog)
KeywordsTRANSCRIPTION / polymerase / elongation factor / nucleosome

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