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Nat Commun. 2017 Mar 7;8:14678. doi: 10.1038/ncomms14678.

α-amino trimethylation of CENP-A by NRMT is required for full recruitment of the centromere.

Author information

1
Department of Biochemistry and Molecular Genetics, University of Virginia, Charlottesville, Virginia 22908, USA.
2
Department of Cell Biology and Cancer, Institut Curie, PSL Research University, CNRS, UMR 144, 26 rue d'Ulm, Paris 75005, France.
3
Northwestern University, Feinberg School of Medicine, Department of Biochemistry and Molecular Genetics, Chicago, Illinois 60611, USA.
4
Robert H. Lurie Comprehensive Cancer Center, Northwestern University Feinberg School of Medicine, Chicago, Illinois 60611, USA.

Abstract

Centromeres are unique chromosomal domains that control chromosome segregation, and are epigenetically specified by the presence of the CENP-A containing nucleosomes. CENP-A governs centromere function by recruiting the constitutive centromere associated network (CCAN) complex. The features of the CENP-A nucleosome necessary to distinguish centromeric chromatin from general chromatin are not completely understood. Here we show that CENP-A undergoes α-amino trimethylation by the enzyme NRMT in vivo. We show that α-amino trimethylation of the CENP-A tail contributes to cell survival. Loss of α-amino trimethylation causes a reduction in the CENP-T and CENP-I CCAN components at the centromere and leads to lagging chromosomes and spindle pole defects. The function of p53 alters the response of cells to defects associated with decreased CENP-A methylation. Altogether we show an important functional role for α-amino trimethylation of the CENP-A nucleosome in maintaining centromere function and faithful chromosomes segregation.

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