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A conserved rRNA methyltransferase regulates ribosome biogenesis


In contrast to the diversity of most ribosomal RNA modification patterns and systems, the KsgA methyltransferase family seems to be nearly universally conserved along with the modifications it catalyzes. Our data reveal that KsgA interacts with small ribosomal subunits near functional sites, including Initiation factor 3 and 50S subunit binding sites. These findings suggest a checkpoint role for this modification system and offer a functional rationale for the unprecedented level of conservation.

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Figure 1: Directed hydroxyl radical probing of 30S subunits from KsgA.
Figure 2: Solution hydroxyl radical footprinting of KsgA on 30S subunits analyzed by primer extension.
Figure 3: A model of KsgA–30S subunit interaction.

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We thank E. Phizicky and the members of the Rife and Culver laboratories for comments on the manuscript. We thank H. Noller (University of California, Santa Cruz, USA) for supplying the IF3 plasmid. This work was supported by the US National Institute of Health grants GM066900 to J.P.R. and GM62432 to G.M.C.

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Z.X. designed and performed experiments; H.C.O. purified KsgA proteins; J.P.R. docked KsgA on 30S subunits; G.M.C. supervised the experiments. All authors discussed results and contributed to the manuscript.

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Correspondence to Gloria M Culver.

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Supplementary Figures 1 and 2, Supplementary Table 1 and Supplementary Methods (PDF 2933 kb)

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Xu, Z., O'Farrell, H., Rife, J. et al. A conserved rRNA methyltransferase regulates ribosome biogenesis. Nat Struct Mol Biol 15, 534–536 (2008).

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