2. Academic Validation
  3. Molecular basis for histone N-terminal methylation by NRMT1

Molecular basis for histone N-terminal methylation by NRMT1

  • Genes Dev. 2015 Nov 15;29(22):2337-42. doi: 10.1101/gad.270926.115.
Ruoxi Wu 1,  Yuan Yue 1,  Xiangdong Zheng 2,  Haitao Li 3
Affiliations

Affiliations

  • 1 MOE Key Laboratory of Protein Sciences, Center for Structural Biology, Department of Basic Medical Sciences, School of Medicine, Tsinghua University, Beijing 100084, China;
  • 2 MOE Key Laboratory of Protein Sciences, Center for Structural Biology, Department of Basic Medical Sciences, School of Medicine, Tsinghua University, Beijing 100084, China; Tsinghua-Peking Center for Life Sciences, Tsinghua University, Beijing 100084, China;
  • 3 MOE Key Laboratory of Protein Sciences, Center for Structural Biology, Department of Basic Medical Sciences, School of Medicine, Tsinghua University, Beijing 100084, China; Collaborative Innovation Center for Biotherapy, West China Hospital, Sichuan University, Chengdu 610041, China.
PMID: 26543159 DOI: 10.1101/gad.270926.115
Abstract

NRMT1 is an N-terminal methyltransferase that methylates histone CENP-A as well as nonhistone substrates. Here, we report the crystal structure of human NRMT1 bound to CENP-A peptide at 1.3 Å. NRMT1 adopts a core methyltransferase fold that resembles DOT1L and PRMT but not SET domain family histone methyltransferases. Key substrate recognition and catalytic residues were identified by mutagenesis studies. Histone peptide profiling revealed that human NRMT1 is highly selective to human CENP-A and fruit fly H2B, which share a common "Xaa-Pro-Lys/Arg" motif. These results, along with a 1.5 Å costructure of human NRMT1 bound to the fruit fly H2B peptide, underscore the importance of the NRMT1 recognition motif.

Keywords

CENP-A; N-terminal methylation; NRMT1; crystal structure; epigenetic regulation; histone modification.

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