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NRMT is an α-N-methyltransferase that methylates RCC1 and retinoblastoma protein

Author

Listed:
  • Christine E. Schaner Tooley

    (Center for Cell Signaling, University of Virginia School of Medicine)

  • Janusz J. Petkowski

    (Center for Cell Signaling, University of Virginia School of Medicine
    University of Virginia)

  • Tara L. Muratore-Schroeder

    (University of Virginia)

  • Jeremy L. Balsbaugh

    (University of Virginia)

  • Jeffrey Shabanowitz

    (University of Virginia)

  • Michal Sabat

    (University of Virginia)

  • Wladek Minor

    (University of Virginia)

  • Donald F. Hunt

    (University of Virginia
    University of Virginia)

  • Ian G. Macara

    (Center for Cell Signaling, University of Virginia School of Medicine)

Abstract

Alpha-N methylation enzyme Little is known about the function of α-N methylation, an unusual post-translational modification in which the amino-terminal residues of proteins are methylated. One known example is that α-N methylation of the Ran guanine nucleotide-exchange factor RCC1 is required for its association with chromatin. More than 30 years ago, it was suggested that a eukaryotic α-N-specific methyltransferase might exist, and now one has been found in HeLa cells. Schaner et al. describe the first known α-N-methyltransferase, named N-terminal RCC1 methyltransferase (NRMT). They identify the NRMT recognition sequence and several new methylation targets, including the tumour suppressor proteins SET and retinoblastoma protein (Rb). A requirement for α-N-methylation is also shown in normal bipolar spindle formation and chromosome segregation.

Suggested Citation

  • Christine E. Schaner Tooley & Janusz J. Petkowski & Tara L. Muratore-Schroeder & Jeremy L. Balsbaugh & Jeffrey Shabanowitz & Michal Sabat & Wladek Minor & Donald F. Hunt & Ian G. Macara, 2010. "NRMT is an α-N-methyltransferase that methylates RCC1 and retinoblastoma protein," Nature, Nature, vol. 466(7310), pages 1125-1128, August.
    • Handle: RePEc:nat:nature:v:466:y:2010:i:7310:d:10.1038_nature09343
    DOI: 10.1038/nature09343
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