Lysine Methylation Modulates the Interaction of Archaeal Chromatin Protein Cren7 With DNA

Frontiers in Microbiology

Niannian Ding²  Cheng Zhong³  Li Huang⁴  Yindi Chu⁴  Zhenfeng Zhang⁴  Yuanyuan Chen⁵ 

[1] Technology, Tianjin, China;College of Life Sciences, University of Chinese Academy of Sciences, Beijing, China;;State Key Laboratory of Food Nutrition and Safety, Tianjin University of Science &State Key Laboratory of Microbial Resources, Institute of Microbiology, Chinese Academy of Sciences (CAS), Beijing, China;The Research Platform for Protein Sciences, Institute of Biophysics, Chinese Academy of Sciences (CAS), Beijing, China;

关键词: hyperthermophilic archaea;    post-translational modification;    lysine methylation;    chromatin protein;    Cren7;    epigenetic regulation;   

DOI  :  10.3389/fmicb.2022.837737

来源: DOAJ

【 摘 要 】

Cren7 and Sis7d, two chromatin proteins from Sulfolobus islandicus, undergo extensive methylations at multiple lysine residues to various extents. Whether this highly conserved protein serves an epigenetic role in the regulation of the structure and function of the chromosome remains unclear. In the present study, we show that methylation significantly affects Cren7, but not Sis7d, in the ability to bind DNA and to constrain negative DNA supercoils. Strikingly, methylated Cren7 was significantly less efficient in forming oligomers or mediating intermolecular DNA bridging. Single-site substitution mutation with glutamine reveals that methylation of the four lysine residues (K24, K31, K42, and K48) of Cren7 at the protein-DNA interface, which are variably conserved among Cren7 homologues from different branches of the Crenarchaeota, influenced Cren7-DNA interactions in different manners. We suggest that dynamic methylation of Cren7 may represent a potential epigenetic mechanism involved in the chromosomal regulation in crenarchaea.

【 授权许可】

Unknown