PRMT6-mediated H3R2me2a guides Aurora B to chromosome arms for proper chromosome segregation

Seul Kim, Nam Hyun Kim, Ji Eun Park, Jee Won Hwang, Nayeon Myung, Ki-Tae Hwang, Young A Kim, Chang-Young Jang () and Yong Kee Kim ()
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Seul Kim: Sookmyung Women’s University
Nam Hyun Kim: Catholic Kwandong University
Ji Eun Park: Sookmyung Women’s University
Jee Won Hwang: Sookmyung Women’s University
Nayeon Myung: Sookmyung Women’s University
Ki-Tae Hwang: Seoul National University Boramae Medical Center
Young A Kim: Seoul National University Boramae Medical Center
Chang-Young Jang: Sookmyung Women’s University
Yong Kee Kim: Sookmyung Women’s University

Nature Communications, 2020, vol. 11, issue 1, 1-15

Abstract: Abstract The kinase Aurora B forms the chromosomal passenger complex (CPC) together with Borealin, INCENP, and Survivin to mediate chromosome condensation, the correction of erroneous spindle-kinetochore attachments, and cytokinesis. Phosphorylation of histone H3 Thr3 by Haspin kinase and of histone H2A Thr120 by Bub1 concentrates the CPC at the centromere. However, how the CPC is recruited to chromosome arms upon mitotic entry is unknown. Here, we show that asymmetric dimethylation at Arg2 on histone H3 (H3R2me2a) by protein arginine methyltransferase 6 (PRMT6) recruits the CPC to chromosome arms and facilitates histone H3S10 phosphorylation by Aurora B for chromosome condensation. Furthermore, in vitro assays show that Aurora B preferentially binds to the H3 peptide containing H3R2me2a and phosphorylates H3S10. Our findings indicate that the long-awaited key histone mark for CPC recruitment onto mitotic chromosomes is H3R2me2a, which is indispensable for maintaining appropriate CPC levels in dynamic translocation throughout mitosis.

Date: 2020
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DOI: 10.1038/s41467-020-14511-w

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