G. C. Atkinson

A role for the S4-domain containing protein YlmH in ribosome-associated quality control in Bacillus subtilis

This study identifies YlmH as a novel RQC factor in B. subtilis, showing it can replace RqcP in polyalanine tail addition and is conserved in bacteria lacking RqcP.

Mechanism of phage sensing and abortion by toxin-antitoxin-chaperone systems

This study identifies and characterizes two Escherichia coli TAC systems that mediate antiphage defense by recognizing phage proteins and modifying mRNA to inhibit translation.

Resolution of ribosomal stalling by ABCF ATPases YfmR and YkpA/YbiT

This study identifies the roles of ABCF ATPases YfmR and YkpA/YbiT in resolving ribosomal stalling during protein synthesis in Bacillus subtilis.

The structural basis of hyperpromiscuity in a core combinatorial network of Type II toxin-antitoxin and related phage defence systems

The paper identifies a core combinatorial network of Type II toxin-antitoxin systems, reveals their structural basis for hyperpromiscuity, and validates new TA systems with functional annotations.

Genome-encoded ABCF factors implicated in intrinsic antibiotic resistance in Gram-positive bacteria: VmlR2, Ard1 and CplR

The paper characterizes genome-encoded ABCF proteins in Gram-positive bacteria, showing their roles in intrinsic antibiotic resistance and revealing structural and regulatory mechanisms.

Direct activation of an innate immune system in bacteria by a viral capsid protein

This study identifies a bacterial immune system that directly senses a viral capsid protein through a toxin-antitoxin system, revealing a PAMP-like mechanism for innate immunity in bacteria.

Structural basis for PoxtA-mediated resistance to Phenicol and Oxazolidinone antibiotics

This paper presents cryo-EM structures of PoxtA bound to the ribosome, revealing its mechanism of antibiotic resistance by perturbing tRNA and altering nascent chain conformation.

Panacea: a hyperpromiscuous antitoxin protein domain for the neutralisation of diverse toxin domains

The paper identifies and validates a hyperpromiscuous antitoxin domain, Panacea, capable of neutralizing diverse toxin domains across microbial and bacteriophage TA systems.

RelA-SpoT Homologue toxins pyrophosphorylate the CCA end of tRNA to inhibit protein synthesis

The paper investigates how four RSH toxins inhibit bacterial growth by pyrophosphorylating tRNA, disrupting protein synthesis and amino acid sensing.

Structural basis of resistance to lincosamide, streptogramin A, and pleuromutilin antibiotics by ABCF ATPases in Gram-positive pathogens

The paper determines the structures of ARE ABCF-ribosome complexes from three Gram-positive bacteria and proposes a model for antibiotic resistance mechanisms.

Structural basis for bacterial ribosome quality control

This study identifies RqcH and YabO as factors mediating C-terminal tailing in Bacillus subtilis through cryo-EM structures showing their role in tRNA movement without mRNA or small subunit.

The C-terminal RRM/ACT domain is crucial for fine-tuning the activation of 'long' RelA-SpoT Homolog enzymes by ribosomal complexes

This study shows that the RRM domain in long RSH enzymes is essential for proper ribosome-mediated activation, preventing excessive (p)ppGpp production and cytotoxicity.

A widespread toxin-antitoxin system exploiting growth control via alarmone signalling

The paper identifies toxin-antitoxin systems in bacteria using alarmone signalling, showing how SASs function as toxins and their antitoxins counteract them.

A role for the Saccharomyces cerevisiae ABCF protein New1 during translation termination

This study identifies New1 as a translation termination factor in yeast by showing it binds the ribosome like eEF3 and affects ribosome queuing at stop codons.

Ribosome profiling analysis of eEF3-depleted Saccharomyces cerevisiae

This study uses ribosome profiling to analyze the effects of eEF3 depletion in yeast, finding reduced ribosome density at stop codons and altered ribosome distribution without specific E-site stalling.