Publications by authors named "N S Garaeva"

Macrolactin A (McA) is a secondary metabolite produced by Bacillus species. It has been known for its antimicrobial properties since the late 1980s, although the exact mechanism of its antibacterial activity remains unknown. In this study, we have found that McA is an inhibitor of protein synthesis in bacteria.

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Article Synopsis
  • Ribosome biogenesis is a complex and energy-demanding process, where any small errors can lead to serious consequences for the cell, including death.
  • Biogenesis factors like RimP play a crucial role in this process by assisting the proper assembly of ribosomal proteins and rRNA.
  • This study details how RimP interacts with the 30S ribosomal subunit in Staphylococcus aureus, providing insights into its binding and structural dynamics through advanced techniques like cryo-EM and NMR spectroscopy.
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  • Ribosome biogenesis is a detailed process involving the maturation of ribosomal subunits, which requires the coordination of various proteins, RNAs, and enzymes.
  • The study focuses on ribosomal binding factor A (RbfA), detailing its crystal and NMR structures as well as a cryo-EM visualization of the 30S-RbfA complex.
  • The findings reveal that RbfA's role in ribosomal subunit maturation is similar in bacteria and mitochondria, suggesting potential targets for developing new antibiotics against bacterial infections.
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  • Ribosomal silencing factor S (RsfS) is a key protein that helps shut down ribosomes and supports cell survival during starvation, and is essential for the formation of the large ribosomal subunit.* -
  • RsfS inhibits the binding of the uL14 ribosomal protein to the large subunit, preventing it from joining with the small subunit.* -
  • Recent experiments identified critical amino acid Y98 on RsfS that could be a new target for drug development aimed at treating infections.*
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  • RimP is a crucial 17.7 kDa protein necessary for the maturation and efficient processing of the 30S ribosome's 16S rRNA, being involved in early assembly stages.
  • It helps stabilize the central pseudoknot during the initial steps of 30S subunit maturation, although the exact mechanism remains unclear.
  • The study details the chemical shift assignments of RimP from Staphylococcus aureus, revealing its structure, which includes eight β-strands and three α-helices, and aims to facilitate the discovery of selective inhibitors for bacterial translation.
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