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<p>Abstract</p> <p>Background</p> <p>Bacterial growth and division requires a core set of essential proteins, several of which are still of unknown function. They are also attractive targets for the development of new antibiotics. YsxC is a member of a family of GTPases highly conserved across eubacteria with a possible ribosome associated function.</p> <p>Results</p> <p>Here, we demonstrate by the creation of a conditional lethal mutant that <it>ysxC </it>is apparently essential for growth in <it>S. aureus</it>. To begin to elucidate YsxC function, a translational fusion of YsxC to the CBP-ProteinA tag in the staphylococcal chromosome was made, enabling Tandem Affinity Purification (TAP) of YsxC-interacting partners. These included the ribosomal proteins S2, S10 and L17, as well as the ^β' subunit of the RNA polymerase. YsxC was then shown to copurify with ribosomes as an accessory protein specifically localizing to the 50 S subunit. YsxC depletion led to a decrease in the presence of mature ribosomes, indicating a role in ribosome assembly and/or stability in <it>S. aureus</it>.</p> <p>Conclusions</p> <p>In this study we demonstrate that YsxC of <it>S. aureus </it>localizes to the ribosomes, is crucial for ribosomal stability and is apparently essential for the life of <it>S. aureus</it>.</p>