Specific N-terminal cleavage of ribosomal protein L27 in Staphylococcus aureus and related bacteria.

Academic Article

Abstract

  • Ribosomal protein L27 is a component of the eubacterial large ribosomal subunit that has been shown to play a critical role in substrate stabilization during protein synthesis. This function is mediated by the L27 N-terminus, which protrudes into the peptidyl transferase center. In this report, we demonstrate that L27 in Staphylococcus aureus and other Firmicutes is encoded with an N-terminal extension that is not present in most Gram-negative organisms and is absent from mature ribosomes. We have identified a cysteine protease, conserved among bacteria containing the L27 N-terminal extension, which performs post-translational cleavage of L27. Ribosomal biology in eubacteria has largely been studied in the Gram-negative bacterium Escherichia coli; our findings indicate that there are aspects of the basic biology of the ribosome in S. aureus and other related bacteria that differ substantially from that of the E. coli ribosome. This research lays the foundation for the development of new therapeutic approaches that target this novel pathway.
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    Published In

    Keywords

  • Amino Acid Sequence, Computational Biology, Cysteine Proteases, Escherichia coli, Mass Spectrometry, Models, Molecular, Molecular Sequence Data, Phylogeny, Protein Biosynthesis, Protein Processing, Post-Translational, Ribosomal Proteins, Ribosomes, Sequence Homology, Amino Acid, Staphylococcus aureus
  • Digital Object Identifier (doi)

    Author List

  • Wall EA; Caufield JH; Lyons CE; Manning KA; Dokland T; Christie GE
  • Start Page

  • 258
  • End Page

  • 269
  • Volume

  • 95
  • Issue

  • 2