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Mechanistic insights into recruitment and regulation of the RNA helicase UPF1 in replication-dependent histone mRNA decay

Replication-dependent histone mRNA decay involves the RNA helicase UPF1, the histone stem-loop binding protein SLBP and the exoribonuclease 3’hExo. Here, the authors present evidence for assembly of a degradosome-like complex involving the three proteins and delineate the mechanism that drives their concerted action to achieve histone mRNA decay.

Alexandrina Machado de Amorim
Guangpu Xue
Sutapa Chakrabarti
ResearchOpen Access03 Jan 2026
Nature Communications

Volume: 17, P: 1-20
Structural insights into ribosomal rescue by Dom34 and Hbs1 at near-atomic resolution

mRNA surveillance is essential to maintain homeostasis in eukaryotes and is activated by mRNAs lacking a stop codon. Here the authors describe a high resolution cryo-EM structure of a nonstop complex that shows how arrested ribosome recognition is achieved during Dom34-mediated mRNA surveillance.

Tarek Hilal
Hiroshi Yamamoto
Christian M.T. Spahn
ResearchOpen Access20 Dec 2016
Nature Communications

Volume: 7, P: 1-8
Nucleotide-induced hyper-oligomerization inactivates transcription termination factor ρ

Bacterial transcription factor Rho (ρ) is a key regulator of transcription termination. Here, the authors show that Escherichia coli ρ forms inactive oligomers and filaments in the presence of stress-associated nucleotides (p)ppGpp and ADP.

Bing Wang
Nelly Said
Irina Artsimovitch
ResearchOpen Access15 Feb 2025
Nature Communications

Volume: 16, P: 1-16
The Psu protein of phage satellite P4 inhibits transcription termination factor ρ by forced hyper-oligomerization

Many bacteriophages can modulate host transcription. Here, the authors uncover the anti-termination mechanism of phage satellite P4 protein, Psu. Psu dimers clamp two open rings of the termination factor ρ, promote ρ hyper-oligomerization, and trap nucleotides in ρ’s binding pockets.

Daniela Gjorgjevikj
Naveen Kumar
Markus C. Wahl
ResearchOpen Access09 Jan 2025
Nature Communications

Volume: 16, P: 1-20
Concerted transformation of a hyper-paused transcription complex and its reinforcing protein

Here, authors use cryoEM, biochemistry and molecular dynamics simulations to delineate a functional cycle of RfaH, a universally conserved transcription factor that undergoes a fold-switch during recruitment to the transcribing RNA polymerase.

Philipp K. Zuber
Nelly Said
Stefan H. Knauer
ResearchOpen Access08 Apr 2024
Nature Communications

Volume: 15, P: 1-19
Sm-like protein Rof inhibits transcription termination factor ρ by binding site obstruction and conformational insulation

Said et al. used cryoEM, biochemistry and bioinformatics to uncover how the Sm-like protein Rof regulates transcription termination. Rof binds termination factor ρ, inhibiting ρ ring closure and its association with RNA or transcription complexes.

Nelly Said
Mark Finazzo
Markus C. Wahl
ResearchOpen Access15 Apr 2024
Nature Communications

Volume: 15, P: 1-18
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
A multi-factor trafficking site on the spliceosome remodeling enzyme BRR2 recruits C9ORF78 to regulate alternative splicing

Bergfort et al. use biochemistry, cryoEM, structure-guided mutagenesis, transcriptomics and proteomics to reveal how the intrinsically unstructured C9ORF78 protein binds BRR2 and PRPF8, regulating cassette exons and alternative 3’-splice sites.

Alexandra Bergfort
Marco Preußner
Markus C. Wahl
ResearchOpen Access03 Mar 2022
Nature Communications

Volume: 13, P: 1-16
The δ subunit and NTPase HelD institute a two-pronged mechanism for RNA polymerase recycling

The bacterial helicase-like transcription factor HelD interacts with the RNA polymerase (RNAP) and together with the RNAP δ subunit enhances RNAP cycling. Here, the authors present the cryo-EM structures of the monomeric and dimeric Bacillus subtilis RNAP-δ-HelD complexes and suggest a model for HelD/δ-mediated RNAP recycling and putative hibernation.

Hao-Hong Pei
Tarek Hilal
Markus C. Wahl
ResearchOpen Access18 Dec 2020
Nature Communications

Volume: 11, P: 1-14
Predicting opioid consumption after surgical discharge: a multinational derivation and validation study using a foundation model

Chris Varghese
Luke Peters
Caroline Reinke
ResearchOpen Access26 Aug 2025
npj Digital Medicine

Volume: 8, P: 1-16
Structures of active melanocortin-4 receptor–Gs-protein complexes with NDP-α-MSH and setmelanotide

Nicolas A. Heyder
Gunnar Kleinau
Patrick Scheerer
ResearchOpen Access24 Sept 2021
Cell Research

Volume: 31, P: 1176-1189

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