| 2021 |
ELOF1 constitutively interacts with RNAPII close to K1268 and acts as a specificity factor that binds and positions the CRL4CSA ubiquitin ligase for optimal ubiquitylation of RNAPII at K1268 during transcription-coupled repair (TCR). ELOF1 loss prevents RNAPII ubiquitylation and downstream TCR factor assembly. |
CRISPR screen, Co-IP, drug-genetic interaction screening, cell biology |
Nature cell biology |
High |
34108663
|
| 2021 |
ELOF1 promotes recruitment of TC-NER factors UVSSA and TFIIH to transcription-blocking lesions, enabling efficient repair and transcription resumption after DNA damage. ELOF1 also modulates transcription to protect cells against transcription-mediated replication stress and genome instability. |
Genome-wide CRISPR-Cas9 screen, immunofluorescence, transcription recovery assays, replication stress assays |
Nature cell biology |
High |
34108662
|
| 2024 |
Cryo-EM structural analysis showed that ELOF1 serves as an adaptor to stably position UVSSA and CRL4CSA on arrested Pol II, leading to ligase neddylation and activation of Pol II ubiquitylation. In the presence of ELOF1, a TFIIS-like element in UVSSA becomes ordered and extends through the Pol II pore, preventing reactivation of Pol II by TFIIS. |
Cryo-electron microscopy, biochemical assays, cell biology, mutagenesis |
Nature structural & molecular biology |
High |
38316879
|
| 2024 |
The yeast ELOF1 ortholog Elf1 promotes Rad26 (CSB ortholog) interactions with lesion-arrested Pol II. Cryo-EM structure of lesion-arrested Pol II-Rad26-Elf1 complex revealed that Elf1 induces additional interactions between Rad26 and lesion-arrested Pol II compared to other forms of stalled Pol II, facilitating TC-NER initiation. |
Cryo-EM structure determination, biochemical assays, genetic complementation |
Proceedings of the National Academy of Sciences of the United States of America |
High |
38194460
|
| 2024 |
Cell-free reconstitution of TC-NER in frog egg extract demonstrated that ELOF1 is required for error-free repair of a site-specific lesion in a transcribed plasmid, establishing ELOF1 as an essential factor in the in vitro TC-NER reaction alongside CSB, CRL4CSA, and UVSSA. |
Cell-free TC-NER reconstitution in Xenopus egg extract, site-specific lesion plasmid, depletion assays, cryo-EM |
Cell |
High |
39547228 39547229
|
| 2024 |
ELOF1 is required for RNAPII ubiquitylation but STK19 loss does not impair this step; STK19 acts downstream of ELOF1-facilitated ubiquitylation to facilitate clearance of lesion-stalled RNAPII. ELOF1 functions together with UVSSA and STK19 to properly recruit and position TFIIH for lesion processing. |
Cryo-EM, mutational analysis, live-cell imaging of RNAPII clearance, TC-NER assays |
Cell |
High |
39547228 39547229
|
| 2025 |
ELOF1 stabilizes paused RNAPII at transcription barriers on antibody gene loci, providing a platform for AID-mediated transcription-coupled DNA damage. ELOF1 deficiency causes paused RNAPII to detach from chromatin, preventing recruitment of factors needed for both AID-induced damage and subsequent repair, resulting in defective class switch recombination and somatic hypermutation in mice. |
Genetic screen in B cells, mouse knockout, ChIP, proximity ligation, biochemical fractionation |
Molecular cell |
High |
40049160 40049162
|
| 2025 |
ELOF1 must bind to RNAPII to serve as a proximity partner for AID and to function in somatic hypermutation and class switch recombination. Loss of ELOF1 reduces RNAPII pausing downstream of transcription start sites and reduces levels of serine-5 (but not serine-2) phosphorylated RNAPII throughout transcribed genes. |
Genetic complementation with RNAPII-binding mutants, ChIP-seq for RNAPII phospho-forms, proximity ligation assay |
Molecular cell |
High |
40049160 40049162
|
| 2020 |
CRISPR screen identified ELOF1 as an RNAPII component whose loss modulates the response to transcription-blocking DNA-damaging agents, placing ELOF1 in the DNA damage response pathway for transcription-blocking lesions. |
CRISPR-Cas9 screen against genotoxic agents in RPE1 cells |
Cell |
Medium |
32649862
|
| 2019 |
Mouse knockout of Elof1 results in peri-gastrulation lethality with developmental delay and morphological defects, and Elof1 regulates mutually exclusive exon use in vivo, suggesting a role in alternative splicing distinct from the yeast ortholog function. |
Mouse loss-of-function allele, phenotypic analysis, splice variant analysis |
PloS one |
Medium |
31276560
|
| 2025 |
ChIP-cryoEM of transcribing RNAPII complexes isolated from human nuclei determined cryo-EM structures of RNAPII elongation complexes associated with genomic DNA in distinct forms, including complexes with ELOF1 and SPT4/5 or SPT6, revealing the structural context of ELOF1 within the elongation complex on chromatin. |
Chromatin immunopurification coupled to cryo-EM (ChIP-cryoEM) from human nuclei |
Nature communications |
Medium |
40436841
|
| 2025 |
Cryo-EM structure of the activated Pol II elongation complex with IWS1 and ELOF1 showed that IWS1 transcription stimulation requires interactions with the RPB2 lobe and ELOF1, indicating ELOF1 cooperates with IWS1 to stimulate Pol II elongation velocity. |
Cryo-EM, in vitro transcription assays, rapid depletion (multi-omics kinetics) |
Nature communications |
Medium |
40835814
|
| 2026 |
ELOF1 is a core component of the promoter-proximal paused RNAPII complex. ELOF1 is enriched at the promoter-proximal region of genes; its rapid degradation reduces pause duration in cells. In reconstituted assays, ELOF1 potently enhances pausing induced by DSIF and NELF at physiological nucleotide concentrations. Cryo-EM structures show that DSIF-NELF-ELOF1 sterically clashes with TFIIF on RNAPII, and RNAPII-DSIF-NELF-ELOF1 (but not RNAPII-DSIF-NELF) counteracts positive effects of TFIIF. |
Rapid protein degradation (auxin-inducible), ChIP-seq/PRO-seq, cryo-EM, in vitro reconstituted pausing assays |
bioRxivpreprint |
High |
42244727
|
| 2026 |
RNAPII ubiquitylation by CSB and CRL4CSA is essential for RNAPII clearance from damage sites; downstream of this ubiquitylation, ELOF1 (together with UVSSA and STK19) is required for proper TFIIH recruitment and positioning, enabling XPD helicase-driven RNAPII dissociation as the primary rapid clearance route. |
Time-resolved RNAPII clearance assay, live-cell imaging, genetic KO of TCR factors, VCP inhibition |
Nature communications |
High |
41554717
|