Writing in Nature Metabolism, Guhathakurta et al. provide pertinent functional and mechanistic insight about this elusive role. Initially using inducible knockouts in primary mouse embryonic fibroblasts (MEFs), the authors show that loss of MOF or KANSL2 leads to aberrant cellular respiration, excessive mitochondrial reactive oxygen species (mtROS) and reduced mitochondrial potential, concomitantly

TDP-43 is a conserved RNA-binding protein. In healthy cells, TDP-43 resides mainly in the nucleus where it plays a role in RNA processing, but it can be shuttled to the cytoplasm as well. In disease, full-length and truncated TDP-43 is post-translationally modified and forms granulofilamentous assemblies. The existence of rare pathogenic missense mutations in the TDP-43 encoding gene in ALS and FTLD

Writing in Nature, Moger-Reischer et al.1 address this question by studying minimal cells from the Mycoplasma mycoides JCVI-syn3B strain. First, they test how reducing protein coding genes from the approximately 900 found in the original strain (non-minimal cell) to less than 500 in the streamlined strain (minimal cell) affects mutation input. Surprisingly, both strains display similar mutation rates

In January 2024, Nature Structural & Molecular Biology (NSMB) will celebrate the 30th anniversary of publishing its first issue . Though initially launched as Nature Structural Biology in 1994, the journal has since expanded its scope to include all research into the molecular underpinnings of life, with the vision that the broadest insight can be gleaned through a suite of complimentary approaches