Telomeric TRF1 controls the transcriptional programmes of pluripotent stem cells by recruiting PRC2 to pluripotency and differentiation genes by controlling the expression of those gene sites and the binding of TERRA RNAs to them.

TRF1 suppresses replication fork stalling, which triggers break induced replication at telomeres associated with DNA damage response, alteration in the telomere chromatin environment, and re-localisation of telomeres to PML bodies.

An atomic model of the 3744-residue Tra1 protein reveals multiple transcription activator binding sites, its integration within the SAGA chromatin coactivator complex, and a striking similarity to DNA-repair factor DNA-PKcs.

Natural Tr1-like cells do not form a functionally stable memory response to allergens, and this instability may limit efforts to re-establish tolerance by expanding Tr1.

A molecular model of the assembled COPI coat, determined by cryo-electron tomography of an in vitro reconstituted budding reaction, reveals details of interactions mediating coat assembly and shows the binding site of ArfGAP2.

Cryo-electron microscopy has been used to provide a structural interpretation of the complete action cycle of release factor 3 during translation termination, which includes a coordinated sequence of interactions with a class-I release factor and the ribosome.

Peptidase activity of DDI2 is required to activate Nrf1 in order to enable proteasome recovery in response to proteasome inhibition.

The enzyme p97/VCP regulates the activity of the transcription factor Nrf1 to promote increased transcription of genes that encode proteasome subunits following inhibition of the proteasome.

TATA-box binding protein is not required for RNA Polymerase II transcription in mouse embryonic stem cells.

Rtf2 is shown to associate with multiple splicing factors and influence splicing of a subset of introns explaining why previous work erroneously assigned it as a replication restart factor in fission yeast.