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

Christine E. Schaner Tooley (), Janusz J. Petkowski, Tara L. Muratore-Schroeder, Jeremy L. Balsbaugh, Jeffrey Shabanowitz, Michal Sabat, Wladek Minor, Donald F. Hunt and Ian G. Macara
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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
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
Ian G. Macara: Center for Cell Signaling, University of Virginia School of Medicine

Nature, 2010, vol. 466, issue 7310, 1125-1128

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.

Date: 2010
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DOI: 10.1038/nature09343

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