Lysine Methylation Modulates the Interaction of Archaeal Chromatin Protein Cren7 With DNA.
Lysine Methylation Modulates the Interaction of Archaeal Chromatin Protein Cren7 With DNA.
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DOI：
10.3389/fmicb.2022.837737
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发表时间：
2022
影响因子：
5.2
通讯作者：
Zhang Z
中科院分区：
文献类型：
--
作者：
Ding N;Chen Y;Chu Y;Zhong C;Huang L;Zhang Z
岛上硫磺的两个染色质蛋白Cren7和Sis7d在多个赖氨酸残基上发生不同程度的广泛甲基化。这种高度保守的蛋白是否在染色体结构和功能的调控中起表观遗传作用尚不清楚。在目前的研究中，我们发现甲基化显著影响Cren7结合DNA和限制负DNA超级线圈的能力，而不是Sis7d。引人注目的是，甲基化的Cren7在形成低聚物或介导分子间DNA桥接方面的效率显着降低。谷氨酰胺单位点替代突变表明，Cren7蛋白- dna界面上的4个赖氨酸残基（K24、K31、K42和K48）甲基化以不同方式影响Cren7- dna相互作用，这些残基在Crenarchaeota不同分支的Cren7同源物中保守程度不同。我们认为Cren7的动态甲基化可能代表了crenarchaea染色体调控的潜在表观遗传机制。
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.