Multiple GTPases Participate in the Assembly of the Large Ribosomal Subunit in Bacillus subtilis

50S ribosome biogenesis Ribosomal protein Eukaryotic Ribosome
DOI: 10.1128/jb.01213-06 Publication Date: 2006-11-16T03:29:02Z
ABSTRACT
GTPases have been demonstrated to be necessary for the proper assembly of ribosome in bacteria and eukaryotes. Here, we show that essential YphC YsxC are required large ribosomal subunit biogenesis Bacillus subtilis. Sucrose density gradient centrifugation subunits isolated from YphC-depleted cells YsxC-depleted indicates they similar 45S intermediate previously identified RbgA-depleted cells. The sedimentation large-subunit was identical found cells, while sedimented slightly slower than 45S, suggesting it is a novel intermediate. Analysis protein composition intermediates either or indicated L16 L36 missing. Purified able interact with vitro, supporting direct role these two proteins 50S subunit. Our results indicate that, as has Saccharomyces cerevisiae biogenesis, bacterial requires function multiple GTPases.
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