Letter abstract
Nature Cell Biology 9, 596 - 603 (2007)
Published online: 15 April 2007 | doi:10.1038/ncb1572
N-terminal 
-methylation of RCC1 is necessary for stable chromatin association and normal mitosis
Ting Chen1, Tara L. Muratore2, Christine E. Schaner-Tooley1, Jeffrey Shabanowitz2, Donald F. Hunt2,3 & Ian G. Macara1
Regulator of chromatin condensation 1 (RCC1) is the only known guanine nucleotide-exchange factor for the Ran GTPase and has pivotal roles in nucleo-cytoplasmic transport, mitosis, and nuclear-envelope assembly1. RCC1 associates dynamically with chromatin through binding to histones H2A and/or H2B in a Ran-regulated manner2, 3. Here, we report that, unexpectedly, the amino-terminal serine or proline residue of RCC1 is uniquely methylated on its 
-amino group. Methylation requires removal of the initiating methionine, and the presence of proline and lysine at positions 3 and 4, respectively. Methylation-defective mutants of RCC1 bind less effectively than wild-type protein to chromatin during mitosis, which causes spindle-pole defects. We propose a bimodal attachment mechanism for RCC1 in which the tail promotes stable RCC1 association with chromatin through DNA binding in an -N-methylation-dependent manner. These data provide the first known function for N-terminal protein methylation.
- Department of Microbiology, Center for Cell Signaling, University of Virginia School of Medicine University of Virginia, Charlottesville, VA 22908–0577, USA.
- Department of Chemistry, University of Virginia, Charlottesville, VA 22904–4319, USA.
- Department of Pathology, University of Virginia, Charlottesville, VA 22908–0904, USA.
Correspondence to: Ian G. Macara1 e-mail: igm9c@virginia.edu
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