PML bodies articles from across Nature Portfolio

The Bloom syndrome helicase (BLM) unwinds a variety of complex DNA structures including G quadruplex. Here the authors report RNF111-ARKL1-dependent ubiquitination of BLM in PML NBs, which limits BLM protein levels and maintains G quadruplex abundance in the nucleus.

Membraneless organelles (MLOs) contribute to intracellular compartmentalization and to various cellular processes. This Review provides a guide to MLOs involved in gene regulation in eukaryotes, discussing their assembly, structure, roles in transcription, RNA processing and translation — particularly in stress conditions — and their disease relevance.

Here the authors identify novel PML-partners and demonstrate that PML NBs control their sumoylation and that PML-controlled sumoylation of transcriptional regulators maintains the embryonic stem cell transcriptome and transposable element silencing.

The transcription factor Aire mediates tissue-specific antigen expression in the thymus for T cell central tolerance induction. Here the authors show that Aire, via its CARD domain, forms multimers that can misdirect Aire to PML bodies leading to the loss of Aire transcriptional activity and induction of autoimmunity.

FAT10 is an ubiquitin-like modifier that targets proteins to proteasomal degradation. Here, the authors show that FAT10 also regulates SUMO activation in vitro and in cells, providing evidence for functional crosstalk between two ubiquitin-like modifiers.

Promyelocytic leukemia protein (PML) is the scaffolding protein that organizes PML nuclear bodies. Here the authors determine the crystal structure of a PML B1-box multimer and characterise the oligomerisation behaviour of the PML RBCC construct and show that disrupting B1-B1 interactions precludes promyelocytic leukemia leukemogenesis in transgenic mice.

A specific nuclear PML isoform functions in the host response to infection by sequestering the viral polymerase of an RNA virus for which replication takes place in the cytoplasm.

The interior of the eukaryotic cell nucleus is populated by a multitude of microscopic domains termed nuclear bodies. Despite having attracted much attention, how these compartments form and are maintained remained elusive. Now, two live-cell imaging studies provide compelling evidence that nascent RNAs can act as transiently immobilized scaffolds that recruit specific nuclear body proteins.