Many trans-acting factors that aid in ribosome biogenesis have been identified in higher organisms but relatively few such factors are known in prokaryotes. In bacteria, the list of such factors includes ATP-energized helicases and chaperones as well as an emerging cadre of switch GTPases. The KsgA protein is a universally conserved methyltransferase that dimethylates both A1518 and A1519 of the 16S rRNA of the small ribosomal subunit. Methylation has long been thought to be solely for fine-tuning of protein translation. In this issue of Molecular Microbiology, Connolly et al. present data suggesting KsgA might function in the assembly of the small subunit of the ribosome. Indeed, the work indicates that KsgA might have a checkpoint role in ribosome biogenesis where methylation by this protein marks the completion of its assembly role. These findings open our thinking to new candidate assembly factors and provide a new direction for understanding ribosome assembly.