In a study published in Nature CommunicationsResearchers at the Karolinska Institute provide insights into a series of events leading to the formation of functional mitribosomes, highlighting the mechanism of action of the nine mitribosome assembly factors involved in this process. The results may help create new opportunities for diagnosis and therapeutic intervention in cancer and diabetes as well as mitochondrial disease.
Mitochondria, the power plant of our cells, convert nutrients into biochemical energy. The large protein complex that performs this conversion task is made within the mitochondria by a dedicated protein factory called the mitochondria. Mutations that affect the mitribosome and its biosynthetic pathway cause severe human mitochondrial disease. However, the biosynthetic pathways of human mitribosomes remain under-examined.
Current research is published in scientific journals Nature CommunicationsResearchers at the Karolinska Institute have solved a high-resolution cryo-electron microscopy called cryo-EM, which solves the high-resolution structure trapped by human mitribosomes during the assembly process. Their research provides insight into a series of events leading to the formation of functional mitribosomes and sheds light on the mechanism of action of the nine mitribosome assembly factors involved in this process.
In addition, cryoEM data revealed an unexpected role for the translational elongation factor mtEF-Tu in mitribosome assembly. Specifically, apart from its active role in protein synthesis, mtEF-Tu also regulates the binding of GTPBP5, one of the assembly factors during mitribosome biogenesis.
Results provide a molecular understanding of mitochondrial disease
Since mitochondrial dysfunction Protein synthesis Cancer, diabetes, Neurodegenerative diseasesA large group of clinically diverse disorders called, and Mitochondrial diseaseThe results may help create new opportunities for diagnostic and therapeutic interventions.
“Our data shed light on the mechanisms of action of many assembly factors that provide the long-awaited structural characterization and reveal new exciting evolutionary adaptations of the human mitochondrial translation system,” said Karolinska, a medical student. Joanna Robach, an assistant professor in the Department of Chemistry and Biophysics, said. Institute, one of the senior authors of the study.
“This study has contributed significantly to our understanding of the complex processes of. Mitribosome Biosynthesis helps us better understand human diseases and the development of new therapies, “said Martin Hällberg, principal investigator in the Department of Cellular and Molecular Biology, one of the senior authors of the study.
Miriam Cipullo et al, Structural basis of late maturation of the large human mitochondrial subunit, Nature Communications (2021). DOI: 10.1038 / s41467-021-23617-8
Quote: 3D (2021, June 16) mitochondrial ribosome assembly was obtained from https: //phys.org/news/2021-06-mitochondrial-ribosome-3d.html on June 16, 2021.
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