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

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.

• Authors: Xiaoxia Dai, Koichiro Otake, Changjun You, Qian Cai, Zi Wang, Hiroshi Masumoto, Yinsheng Wang
• Journal: Journal of proteome research (J Proteome Res) Vol. 12 Issue 9 Pg. 4167-75 (Sep 06 2013) ISSN: 1535-3907 [Electronic] United States
• PMID: 23978223 (Publication Type: Journal Article, Research Support, N.I.H., Extramural, Research Support, Non-U.S. Gov't)

Chemical References

• Centromere Protein B
• DNA
• Methyltransferases
• NTMT1 protein, human

Topics

• Amino Acid Sequence
• Animals
• Centromere (metabolism)
• Centromere Protein B (chemistry, metabolism)
• DNA (metabolism)
• Gene Expression
• HEK293 Cells
• Humans
• Methylation
• Methyltransferases (chemistry, genetics, metabolism)
• Mice
• Protein Binding
• Protein Processing, Post-Translational
• Protein Structure, Tertiary