A massive supercomplex in mitochondria comprising all four respiratory complexes induces a membrane curvature necessary for proper mitochondrial function. The supercomplex assembly actively contributes to the shaping of the macroscopic architecture of mitochondria.
Researchers have uncovered a dynamic mechanism for mitoribosomal small subunit biogenesis and preinitiation. The study's findings reveal a multistep assembly pathway controlled by an allosteric mechanism, with essential modifications occurring at each step.
A new study uses electron cryo-microscopy to reveal the molecular mechanism of bioenergetic protein synthesis in human mitochondria, revealing a more flexible and active mitoribosome than previously thought. The discovery sheds light on how medical disorders such as deafness and cancer development are linked to mitochondrial function.
A recent study published in the EMBO Journal has provided new insights into the formation of mitoribosomes, revealing a complex network of assembly factors that shield the sensitive ribosomal core. The researchers identified five key assembly factors that are conserved across different species, including humans.
Cryo-EM studies have identified different types of ATP synthase organization, including a symmetry-deviated dimer and hexamer assemblies. These structures shape the bioenergetic membrane and are critical for maintaining bioenergetics in Apicomplexa.
Researchers develop Single-residue Terminal Labeling (STELLA) to fluorescently tag microproteins without disrupting their function. The method enables visualization of elusive polypeptides from SARS-CoV2 coronavirus, opening new avenues for studying tiny proteins in living cells.
Researchers discovered a mechanism where histone variant H3.3 is replenished to silence transposons in pluripotent stem cells, potentially linked to cancer tumorigenesis
Researchers have reconstructed a ciliate mitoribosome using cryo-EM, identifying nine novel proteins encoded in the mitochondrial genome and challenging existing views on mitochondrial translation evolution. The discovery provides new insights into mitochondria's structural and functional complexity.
Researchers have developed a method to label and image cell surface receptors on live cells with two different colors, allowing for the study of receptor dynamics and pharmacology in their native setting. This innovation expands the possibilities for studying G-protein coupled receptors and other important drug targets.
Researchers discovered diverse forms of Photosystem I in cyanobacteria and algae, including a specialized dimer in Anabaena and a minimal form in Dunaliella. These findings suggest new energy pathways, pigment binding sites, and phospholipids, providing insight into photosynthesis beyond traditional textbook descriptions.
Researchers have determined the atomic model of mitochondrial ATP synthase in a single-cell photosynthetic organism, Euglena gracilis. The study reveals new insights into the structure and function of this essential energy production machinery.
A team of researchers from SciLifeLab and AstraZeneca have used cryo-EM to unravel the extracellular region of the receptor tyrosine kinase RET, which is involved in degenerative diseases. The study reveals how two large RET monomers dimerize on the membrane, leading to potential therapeutic targets for neuronal survival.