The first dipteran luciferase from Keroplatus testaceus evolved by repurposing of a storage protein.

BIOINFORMATIC AND FUNCTIONAL CHARACTERIZATION OF THE VITELLOGENIN RECEPTOR IN DIPETALOGASTER MAXIMA, A VECTOR OF CHAGAS DISEASE.

DmaxVgR gene silencing disrupted follicular architecture and reduced vitellogenin uptake by the oocytes, resulting in increased vitellogenin levels in the hemolymph suggest a feedback mechanism regulating YPP production.

in silico Analysis of Phycodnaviridae Tetrapyrrole Enzymes: Subcellular Localization and Functional Divergence from Host Homologs

Evolutionary hijacking of fatty acid biosynthesis drives insecticidal acylsugar diversity in tomato

The evolution of plant defensive specialized metabolites often involves repurposing existing primary metabolic pathways for novel roles. However, the relative contribution of changes in protein function versus gene regulation and localization in driving such divergency remains less well understood. Here, we investigate the evolutionary origin of long-branched-chain acylsugars—a class of insecticidal metabolites found in wild tomatoes but absent from their domesticated counterpart. We show that this chemical divergency is enabled by a single enzyme, an acyl-CoA synthetase (SpBACS1), that was repurposed to bridge two distinct primary metabolic pathways. We demonstrate that SpBACS1 activates products of amino acid catabolism and primes them as non-canonical starters for elongation by the plastidial fatty acid synthase machinery for acylsugar assembly. Strikingly, the loss of this trait during domestication was not due to impaired enzyme function. Instead, we describe two distinct regulatory mechanisms. First, the cultivated ortholog, SlBACS1, lacks expression in acylsugar-producing trichomes due to promoter sequence divergence, despite retaining enzyme catalytic activity. Concurrently, their paralogs, BACS2, were neolocalized to the mitochondria, functionally isolating them from the chloroplast-based primary fatty acid metabolic elongation pathway. These findings demonstrate how divergence in cis-regulatory elements and subcellular targeting, in the absence of protein function modification, were potent drivers of metabolic evolution, providing a strategy for re-engineering valuable chemical diversity into cultivated crops. Long-branched-chain acylsugars are insecticidal metabolites found in wild tomatoes but not their domesticated counterpart. Here the authors show changes in expression and localization of a key enzyme is responsible for this difference.

Aerolysin-like proteins from Armillaria ostoyae with potential roles in plant pathogenicity reveal a distant evolutionary relationship to toadfish natterins

Understanding the evolutionary distribution and functional roles of toxins across diverse taxa remains a fundamental challenge in fungal biology. Aerolysin-like beta-pore-forming toxins are widely distributed across multiple kingdoms of life, yet their specific occurrence and structural diversity within the fungal kingdom remain poorly characterized. In our current study, we address this gap by investigating candidate aerolysin-like proteins in the basidiomycete Armillaria ostoyae using an integrated framework combining structural modeling, comparative genomics, and transcriptomic datasets spanning multiple developmental stages. Our results demonstrate that these candidate proteins are actively transcribed throughout the fungal life cycle, with consistent expression maintained in mature fruiting-body tissues. Notably, we show that the specific gene ARMOST_18480 undergoes significant upregulation under plant-invasive conditions, strongly supporting its role as a putative pathogenicity-associated factor. Structural characterization revealed a modular architecture with deeply conserved pore-forming domains including Alanine-Glycine-Isoleucine-Proline (AGIP)-like loop variants homologous to vertebrate natterins from Thalassophryne nattereri, despite low overall sequence identity. Importantly, phylogenetic inference robustly resolves these Armillaria proteins within distinct fungal lineages well-separated from their vertebrate counterparts. Together, these findings significantly expand the known evolutionary distribution of the aerolysin superfamily and identify key candidates for future functional validation regarding pore-forming activity, plant pathogenicity, and mushroom-associated bioactivity.

Molecular and biological characterisation of Magnaporthe oryzae botourmiavirus 15

First glimpses into the molecular kaleidoscope of pyrenoid diversity.

A significant proportion of global photosynthetic carbon fixation relies on the pyrenoid, a biomolecular condensate found in the chloroplast of most unicellular algae, where the CO2-fixing enzyme Rubisco is exposed to saturating concentrations of the gas. In this review, we highlight recent advances in our understanding of the molecular basis of diverse pyrenoids. Phase separation of phylogenetically distant Rubiscos is mediated by convergently evolved linker proteins, with an emerging theme of pyrenoid condensation being organized via Rubisco-binding motifs. To minimize CO2 leakage out of the pyrenoid, starch sheaths and protein shells have evolved to surround the pyrenoid in various algal lineages. Crucially, the pyrenoid is a biomolecular condensate with an increasingly well-defined function that has evolved multiple times over the past billions of years. The emerging similarities and differences of these various pyrenoids will inform our appreciation of phase separation in biology and empower engineering efforts aimed at enhancing photosynthetic CO2 assimilation.