Title: Identification of novel α-n-methylation of CENP-B that regulates its binding to the centromeric DNA.

Authors: Dai, Xiaoxia; Otake, Koichiro; You, Changjun; Cai, Qian; Wang, Zi; Masumoto, Hiroshi; Wang, Yinsheng

Published In J Proteome Res, (2013 Sep 06)

Abstract: The eukaryotic centromere is an essential chromatin region required for accurate segregation of sister chromatids during cell division. Centromere protein B (CENP-B) is a highly conserved protein which can bind to the 17-bp CENP-B box on the centromeric DNA. In this study, we found that CENP-B could be α-N-methylated in human cells. We also showed that the level of the α-N-methylation was stimulated in cells in response to a variety of extracellular stimuli, including increased cell density, heat shock, and arsenite treatment, although the methylation level was not altered upon metaphase arrest. We identified N-terminal RCC1 methyltransferase (NRMT) as a major enzyme required for the CENP-B methylation. Additionally, we found that chromatin-bound CENP-B was primarily trimethylated and α-N-trimethylation could enhance CENP-B's binding to CENP-B box in cells. Our study also expands the function of protein α-N-methylation that has been known for decades and whose function remains largely unexplored.

PubMed ID: 23978223

MeSH Terms: Amino Acid Sequence; Animals; Centromere Protein B/chemistry; Centromere Protein B/metabolism*; Centromere/metabolism*; DNA/metabolism*; Gene Expression; HEK293 Cells; Humans; Methylation; Methyltransferases/chemistry; Methyltransferases/genetics; Methyltransferases/metabolism; Mice; Protein Binding; Protein Processing, Post-Translational*; Protein Structure, Tertiary