bims-resufa Biomed News
on Respiratory supercomplex factors
Issue of 2025–08–31
two papers selected by
Gavin McStay, Liverpool John Moores University



  1. J Cardiovasc Dev Dis. 2025 Aug 20. pii: 318. [Epub ahead of print]12(8):
      Combined oxidative phosphorylation deficiency type 8 (COXPD8) is an autosomal recessive mitochondrial disorder caused by a mutation of the nuclear encoded mitochondrial alanyl-tRNA synthetase gene (AARS2). Clinical manifestations of COXPD8 include lethal infantile hypertrophic cardiomyopathy, pulmonary hypoplasia, generalized muscle weakness, and neurological involvement. We report a patient with COXPD8 caused by two mutations in the AARS2 gene. The c.1738 C>G mutation has not been previously reported, while the c.2872 C>T mutation has been associated with pulmonary hypoplasia and hypertrophic cardiomyopathy. Cardiac tissue, obtained through the LungMAP program, showed that, compared to other patients of similar ages, these two mutations affect not only the assembly of functional monomeric complexes (Cx) I and IV of the electron transport chain (ETC) but also limit the formation of respiratory supercomplexes. This patient had altered expression of some ETC proteins but normal expression of several enzymes of the tricarboxylic acid cycle. We also show that one of the control/comparison patients had an undiagnosed ETC Cx IV deficiency. In conclusion, our data demonstrate that the two mutations of the AARS2 gene are associated with failed assembly of Cx I and Cx IV and reduced formation of respiratory supercomplexes of the ETC, likely leading to acute bioenergetic stress.
    Keywords:  COXPD8; electron transport chain; hypertrophic cardiomyopathy; mitochondrial disease; mitochondrial supercomplexes
    DOI:  https://doi.org/10.3390/jcdd12080318
  2. IUCrJ. 2025 Sep 01. 12(Pt 5): 563-569
      We analyzed ATP synthase dimers in mitochondria purified from four plant species by subtomogram averaging, using Saccharomyces cerevisiae as a control. The purified mitochondria were plunge-frozen and broken mitochondria were examined by electron cryo-tomography. In each case, the ATP synthase dimers formed extensive rows along the tightly curved cristae ridges. ATP synthase dimer particles of each species were picked and averaged. Subtomogram averages of all four plant ATP synthases revealed an extra density at the tip of the peripheral stalk next to the OSCP hinge that is not seen in S. cerevisae. The dimer angle between the ATP synthase monomers is wider than in Polytomella, S. cerevisae or mammals, but less wide than in Caenorhabditis elegans. Slight variations in dimer angle indicate that ATP synthase dimers of plant mitochondria are more flexible than others.
    Keywords:  3D reconstruction and image processing; ATP synthases; cryo-electron microscopy; cryo-electron tomography; macromolecular machines; mitochondria; structure determination; subtomogram averaging
    DOI:  https://doi.org/10.1107/S2052252525006220