To investigate why bats are long-lived and cancer-resistant, multi-omic data from bat and human cells was analyzed using computational flux modeling, suggesting dysregulation of succinate-fumarate dynamics and an ischemic-like basal metabolism in bat cells.

Co-evolving residue pairs in the different components of a protein complex almost always make contact across the protein–protein interface, thus providing powerful restraints for the modeling of protein complexes.

A near-complete flux balance analysis model of a minimal cell demonstrates the high essentiality of its metabolic genes, agrees well with experimental essentiality data and suggests some further gene removals.

Precise control of the bacterial flagellar motor determines bacterial cell dispersal and bacteria-surface interactions.

In the PomX/Y/Z cell division regulatory system, PomX is a PomZ ATPase activating protein, a scaffold for PomX/Y/Z complex formation, and important for fission of the PomX/Y/Z complex during division.

Bacterial small RNAs derived from the 3' untranslated region of an mRNA can serve as autoregulatory elements.

Diverse sophisticated phylogenetic analyses update the phylogeny of the Alphaproteobacteria and show that the parasitic Holosporales is a derived group within the Rhodospirillales order which comprises primarily free-living alphaproteobacteria.

The molecular mechanism of switching between phosphotransferase- and phosphatase-competent states in histidine-kinases has been uncovered, through direct crystallographic observation of bona fide complexes between a histidine-kinase and its response regulator from Bacillus subtilise.

Structural and functional analyses show how the spliceosomal Prp3 protein concomitantly binds double- and single- stranded regions in U4/U6 di-snRNAs and serves to stabilize the U4/U6•U5 tri-snRNP for splicing.

The three-dimensional structures of Mycobacterium tuberculosis cytochrome bcc in complex with the antituberculosis agents, Q203 and TB47, explain how these inhibitors suppress activity of the complex.