Publications by authors named "Ekansh K Agrawal"
Article Synopsis
- Borrelia burgdorferi (Bbu), which causes Lyme disease, affects over 10% of the global population and leads to around 500,000 infections annually in the US.
- Researchers revealed the structure of the Bbu 70S ribosome using advanced cryo-electron microscopy, identifying new ribosomal proteins and suggesting evolutionary links to other species.
- Findings about the Bbu ribosome could improve the design of antibiotics targeting it, potentially enhancing treatments for Lyme disease.
Article Synopsis
- The spirochete bacteria cause Lyme disease, affecting over 10% of the global population and around half a million people in the US each year, with treatment primarily involving ribosome-targeting antibiotics.
- Using advanced cryo-electron microscopy, researchers detailed the 70S ribosome's structure, highlighting the presence of the bbHPF protein and new ribosomal proteins unique to certain bacteria.
- The study suggests evolutionary links between ribosomal proteins and provides insights for designing more effective antibiotics to combat Lyme disease.
Ribosomes are recycled for a new round of translation initiation by dissociation of ribosomal subunits, messenger RNA and transfer RNA from their translational post-termination complex. Here we present cryo-EM structures of the human 55S mitochondrial ribosome (mitoribosome) and the mitoribosomal large 39S subunit in complex with mitoribosome recycling factor (RRF) and a recycling-specific homolog of elongation factor G (EF-G2). These structures clarify an unusual role of a mitochondria-specific segment of RRF, identify the structural distinctions that confer functional specificity to EF-G2, and show that the deacylated tRNA remains with the dissociated 39S subunit, suggesting a distinct sequence of events in mitoribosome recycling.
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