bims-resufa Biomed News
on Respiratory supercomplex factors
Issue of 2026–09–20
two papers selected by
Gavin McStay, Liverpool John Moores University
  1. CryoBN-PAGE: A Rapid and Cost-Effective Method for the Analysis of Yeast Respiratory Complexes and Their Dynamic Organization.
  2. Cox7a2l Variation Influences Complex III and Mitochondrial Supercomplex Differences in 3xTG-AD Mixed-Background Mice.
  1. 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
  2. Int J Mol Sci. 2026 Aug 28. pii: 7710. [Epub ahead of print]27(17):
    Cox7a2l Variation Influences Complex III and Mitochondrial Supercomplex Differences in 3xTG-AD Mixed-Background Mice.
    Wenzhuo Ma, Clarissa Cavarsan, Lauren F Bazinet, Scarlett M Silvia, Joseph Owusu-Sarfo, Janet Atoyan, Judianne Davis, William E Van Nostrand, John K Robinson, Richard T Clements.
      Mitochondrial dysfunction, including impaired respiration and increased reactive oxygen species (ROS), is an early feature of Alzheimer's disease (AD) models. Electron transport chain supercomplexes (mSCs) regulate respiratory efficiency and ROS generation, yet genetic determinants of mSC organization in AD models remain underappreciated. Cox7a2l is known to promote CIII2/CIV association and CIV incorporation into mSCs. We examined the commonly used mixed-background B6;129S 3xTg-AD mice and B6129SF2/J controls aged 12-15 months, as well as specific rat AD models for changes in mSC organization using blue and clear native-PAGE and DIA-MS. BN and CN-PAGE revealed a marked shift toward larger mSC assemblies in 3xTg-AD mice and a distinct ~650 kDa assembly of complex III absent from controls. Gene sequencing showed that 3xTg-AD mice retained the full-length Cox7a2l variant similar to 129S strains, whereas controls predominantly carried a shortened C57BL/6-associated variant. DIA-MS identified greatly increased Cox7a2l in differential mSC bands. Similar changes were found in 3xTg-AD heart tissue. In contrast, AD rat models and their controls, all expressing full-length Cox7a2l, did not exhibit comparable mSC differences. These findings suggest Cox7a2l genotype as a determinant of mSC organization and highlight the need to account for genetic background when interpreting mSC-dependent mitochondrial phenotypes in mixed-background 3xTg-AD studies. This distinction is essential for accurately separating strain-dependent effects from AD-associated mitochondrial changes.
    Keywords:  Alzheimer’s disease; COX7RP; SCAF1; mitochondrial supercomplex; respiration; supercomplex
    DOI:  https://doi.org/10.3390/ijms27177710
This page is being maintained by Thomas Krichel. It was last updated on 2026‒09‒20 at 8:26.