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Correction to “The thymocyte-specific RNA-binding protein Arpp21 provides TCR repertoire diversity by binding to the 3’-UTR and promoting Rag1 mRNA expression”

Meng Xu
Taku Ito-Kureha
Vigo Heissmeyer
Amendments and CorrectionsOpen Access05 Aug 2024
Nature Communications

Volume: 15, P: 1-3
The thymocyte-specific RNA-binding protein Arpp21 provides TCR repertoire diversity by binding to the 3’-UTR and promoting Rag1 mRNA expression

Regulation of thymocyte development by RNA-binding proteins is not fully characterized. Here the authors show the RBP ARPP21 interacting with the Rag1 3’-UTR to promote Rag1 expression, TCR rearrangement and an increased diversity of the TCR repertoire and that ARPP21 is down regulated by TCR stimulation.

Meng Xu
Taku Ito-Kureha
Vigo Heissmeyer
ResearchOpen Access11 Mar 2024
Nature Communications

Volume: 15, P: 1-20
Structural basis for RNA polymerase II ubiquitylation and inactivation in transcription-coupled repair

Here the authors visualize the workings of ELOF1 in transcription-coupled DNA repair, showing that ELOF1 repositions repair factors on the surface of DNA damage-stalled RNA polymerase II to facilitate its ubiquitylation by the CRL4^CSA E3 ligase and inactivation by UVSSA.

Goran Kokic
George Yakoub
Martijn S. Luijsterburg
ResearchOpen Access05 Feb 2024
Nature Structural & Molecular Biology

Volume: 31, P: 536-547
Structural basis of human transcription–DNA repair coupling

The authors resolve the structure of five complexes containing RNA polymerase II and the CSA and CSB proteins, offering insight into how the repair of DNA lesions is coupled to transcription.

Goran Kokic
Felix R. Wagner
Patrick Cramer
ResearchOpen Access15 Sept 2021
Nature

Volume: 598, P: 368-372
Analysis of protein-DNA interactions in chromatin by UV induced cross-linking and mass spectrometry

Cross-linking mass spectrometry (XLMS) allows mapping of protein-protein and protein-RNA interactions, but the analysis of protein-DNA complexes remains challenging. Here, the authors develop a UV light-based XLMS workflow to determine protein-DNA interfaces in reconstituted chromatin and isolated nuclei.

Alexandra Stützer
Luisa M. Welp
Henning Urlaub
ResearchOpen Access16 Oct 2020
Nature Communications

Volume: 11, P: 1-12
Structural basis of TFIIH activation for nucleotide excision repair

The NER machinery contains the multisubunit transcription factor IIH (TFIIH) that opens the DNA repair bubble, scans for the lesion, and coordinates excision of the damaged site. Here the authors resolve the cryo-electron microscopy structure of the human core TFIIH-XPA-DNA complex and provide insights into its activation.

Goran Kokic
Aleksandar Chernev
Patrick Cramer
ResearchOpen Access28 Jun 2019
Nature Communications

Volume: 10, P: 1-9
Extended DNA threading through a dual-engine motor module of the activating signal co-integrator 1 complex

ASCC3 is a multi-functional helicase that contains two consecutive Ski2-like helicase units. Here, the authors show that ASCC3 can unwind DNA by threading one strand of a substrate duplex through both helicase units, supported by the TRIP4 protein.

Junqiao Jia
Tarek Hilal
Markus C. Wahl
ResearchOpen Access05 Apr 2023
Nature Communications

Volume: 14, P: 1-14
Dynamic and flexible H3K9me3 bridging via HP1β dimerization establishes a plastic state of condensed chromatin

Heterochromatin protein 1 (HP1), including HP1 α, β and γ, is a family of non-histone chromatin factors thought to be involved in chromatin organization. Here, the authors show that dimeric HP1β interacts dynamically with H3K9me3, a hallmark of heterochromatin, and bridges condensed chromatin.

Kyoko Hiragami-Hamada
Szabolcs Soeroes
Wolfgang Fischle
ResearchOpen Access19 Apr 2016
Nature Communications

Volume: 7, P: 1-16

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Correction to “The thymocyte-specific RNA-binding protein Arpp21 provides TCR repertoire diversity by binding to the 3’-UTR and promoting Rag1 mRNA expression”

The thymocyte-specific RNA-binding protein Arpp21 provides TCR repertoire diversity by binding to the 3’-UTR and promoting Rag1 mRNA expression

Structural basis for RNA polymerase II ubiquitylation and inactivation in transcription-coupled repair

Structural basis of human transcription–DNA repair coupling

Analysis of protein-DNA interactions in chromatin by UV induced cross-linking and mass spectrometry

Structural basis of TFIIH activation for nucleotide excision repair

Extended DNA threading through a dual-engine motor module of the activating signal co-integrator 1 complex

Dynamic and flexible H3K9me3 bridging via HP1β dimerization establishes a plastic state of condensed chromatin

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