bims-tricox 2026-09-20 papers

Issue of 2026–09–20
two papers selected by
Yash Verma, Universität Zürich

Yeast. 2026 Sep 14.

CryoBN-PAGE: A Rapid and Cost-Effective Method for the Analysis of Yeast Respiratory Complexes and Their Dynamic Organization.

Lizeth J Camacho Lopez, Mazzen H Eldeeb, Elliana G Mohrhardt, Flavia Fontanesi.

Over the last three decades, blue native polyacrylamide gel electrophoresis (BN-PAGE), a technique that allows the resolution of large protein complexes in their native conformations, has profoundly impacted the study of mitochondrial biology and our understanding of oxidative phosphorylation (OXPHOS) system's biogenesis and organization. However, while protein samples for BN-PAGE can be prepared from permeabilized mammalian cells, the analysis of yeast OXPHOS complexes requires the prior isolation of mitochondria from whole yeast cells. This requirement limits high-throughput studies and prevents short time-course analyses. We therefore combined BN-PAGE techniques with the cryogenic milling of snap-frozen cells to develop cryoBN-PAGE, which allows for the preparation of BN-PAGE samples from whole-cell yeast lysates and avoids the cost and time associated with mitochondrial isolation. Here, we show the optimization of the method and demonstrate that it can be efficiently paired with a number of downstream applications, such as immunoblots, second-dimension SDS-PAGE, and in gel enzymatic activity assays. Furthermore, by avoiding the time-consuming mitochondrial isolation, cryoBN-PAGE allows for precise time-course assays and the investigation of rapid changes in the properties of the OXPHOS system in response to alterations in environmental conditions.

Keywords: BN‐PAGE; Saccharomyces cerevisiae; cryo‐milling; electron transport chain; mitochondria; respiratory supercomplex

DOI: https://doi.org/10.1002/yea.70043

J Virol. 2026 Sep 14. e0174625

The factory enters the fray: how mitochondrial protein trafficking shapes the host response to infection.

Dustin C Hancks, Steven F Baker.

Beyond textbook functions in homeostatic metabolism, mitochondria are now recognized as central coordinators of cell-intrinsic and cell-extrinsic immune responses to infection. Directed trafficking of proteins and other molecules between mitochondria and the rest of the cell underlies a growing catalog of these activities. Some are pro-host; others are antagonized by viral effectors or co-opted by viruses entirely. How host and viral factors rewire the mitochondrial proteome during infection to shape these outcomes remains incompletely understood. The evolutionary history of this system adds another dimension: mitochondria retain biochemical signatures of their α-proteobacterial endosymbiotic origin, and ongoing co-evolution between viral, host, and mitochondrial genomes continues to shape the proteins that traffic to and from the organelle. Using published examples, we highlight general principles, mechanisms, and consequences of host and viral protein localization to and from the mitochondria. To support discovery, we present integrated gene lists identifying host mitochondrial factors with evidence for type I interferon stimulation, interactions with viral proteins, and signatures of positive selection. Together, these resources and the principles within offer a framework for understanding mitochondria not as passive metabolic machinery but as actively contested cellular territory whose protein composition is continuously negotiated between the host and the pathogen.

Keywords: adaptation; immunometabolism; mitochondria; protein localization; viruses

DOI: https://doi.org/10.1128/jvi.01746-25