Brief Communication | Published:

A conserved rRNA methyltransferase regulates ribosome biogenesis

Nature Structural & Molecular Biology volume 15, pages 534536 (2008) | Download Citation

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Abstract

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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Acknowledgements

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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Affiliations

  1. Department of Biology, Hutchison Hall 301, University of Rochester, Rochester, New York 14627, USA.

    • Zhili Xu
    •  & Gloria M Culver
  2. Department of Medicinal Chemistry and Institute for Structural Biology and Drug Discovery, 800 East Leigh Street, Virginia Commonwealth University, Richmond, Virginia 23298, USA.

    • Heather C O'Farrell
    •  & Jason P Rife

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Contributions

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.

Corresponding author

Correspondence to Gloria M Culver.

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    Supplementary Text and Figures

    Supplementary Figures 1 and 2, Supplementary Table 1 and Supplementary Methods

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DOI

https://doi.org/10.1038/nsmb.1408

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