bims-resufa Biomed News
on Respiratory supercomplex factors
Issue of 2026–03–15
two papers selected by
Gavin McStay, Liverpool John Moores University
  1. Roles of mitochondrial complexes in non-alcoholic fatty liver disease.
  2. An efficient clear-native PAGE-based workflow for cryo-electron microscopy sample preparation of large protein complexes.
  1. Front Mol Biosci. 2026 ;13 1752024
    Roles of mitochondrial complexes in non-alcoholic fatty liver disease.
    Kai Wang, Li Wang, Jiamin Ning, Dexin Li.
      Non-alcoholic fatty liver disease (NAFLD) is increasingly recognized as a mitochondrial-driven metabolic disorder, yet the specific contributions of individual mitochondrial respiratory chain complexes remain poorly defined. In particular, inconsistent alterations in complexes I-V have been reported across different NAFLD models, representing a critical knowledge gap. Here, we systematically reviewed in vivo and in vitro studies to evaluate changes in mitochondrial complexes I-V during NAFLD progression. Overall, NAFLD is commonly associated with reduced complex activity, impaired mitochondrial respiration, and increased reactive oxygen species production. Notably, a subset of studies reported enhanced complex activity and respiration, suggesting context-dependent mitochondrial adaptations. This synthesis clarifies divergent findings and highlights mitochondrial respiratory complexes as dynamic and therapeutically relevant targets for future NAFLD intervention strategies.
    Keywords:  energy metabolism; lipid metabolism; mitochondrial complexes; non-alcoholic fatty liver disease (NAFLD); redox homeostasis
    DOI:  https://doi.org/10.3389/fmolb.2026.1752024
  2. Plant Methods. 2026 Mar 10.
    An efficient clear-native PAGE-based workflow for cryo-electron microscopy sample preparation of large protein complexes.
    Zitong Yang, Shinsa Kameo, Soichiro Seki, Genji Kurisu, Ryouichi Tanaka, Akihiro Kawamoto, Atsushi Takabayashi.
       BACKGROUND: Cryo-electron microscopy (cryo-EM) has revolutionized protein research by enabling high-resolution structural analysis. However, preparing ultra-large protein complexes (e.g., > 700 kDa) for cryo-EM remains challenging, as it requires preserving both structural integrity and the native state. Conventional isolation methods, such as sucrose density gradient centrifugation, require large sample volumes and provide limited separation resolution. In contrast, native PAGE offers higher resolution; however, no established method exists for extracting protein complexes from gels followed by further purification to achieve high purity. Consequently, no standardized native PAGE-based protocol for cryo-EM sample preparation avoids multiple purification steps. Hence, we aimed to develop a rapid and efficient cryo-EM protein sample preparation method using electroelution with an optimized buffer system that preserves complex integrity to recover target protein complexes after sodium deoxycholate (DOC)-based clear-native PAGE (CN-PAGE).
    RESULTS: We developed an agarose-acrylamide composite gel, which is simpler to prepare and mechanically more robust than conventional linear-gradient acrylamide gels commonly used for CN-PAGE, facilitating precise band excision for efficient electroelution. Cryo-EM structural analysis of the photosystem I-light-harvesting complex I (PSI-LHCI) supercomplex from Arabidopsis thaliana achieved high resolution (2.18 Å) after electroelution from this gel, requiring only buffer exchange by ultrafiltration to remove DOC before grid preparation, without additional chromatographic purification. This finding suggests that DOC may be the main inhibitor of successful grid preparation.
    CONCLUSION: Our results demonstrate the potential of this method for isolating large protein complexes from small sample volumes for cryo-EM structural analysis. This approach may expand the scope of cryo-EM targets to include some challenging systems previously hindered by purification difficulties.
    Keywords:  Clear-native PAGE; Cryo-EM; Electroelution; Photosystem; Protein complex
    DOI:  https://doi.org/10.1186/s13007-026-01513-w
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