SUMO 化组蛋白 H4 的全化学合成揭示了与组蛋白泛素化的负生化交叉对话。
Total chemical synthesis of sumoylated histone H4 reveals negative biochemical crosstalk with histone ubiquitylation.
机构信息
Department of Chemistry, University of Washington, Seattle 98195, USA.
Department of Pharmacology, University of Washington; Howard Hughes Medical Institute, University of Washington, Seattle 98195, USA.
出版信息
Chem Commun (Camb). 2023 Mar 30;59(27):4063-4066. doi: 10.1039/d2cc06683a.
Abstract
An efficient total chemical synthesis of site-specifically sumoylated histone H4 was undertaken to generate homogenously modified mononucleosomes. These were tested as substrates in biochemical assays with the histone H2B-specific ubiquitin ligases Rad6 and Bre1, which revealed the strong inhibition of H2B ubiquitylation by SUMO. This novel negative biochemical crosstalk between SUMO and ubiquitin was also confirmed to exist in human cells.
摘要
我们进行了高效的组蛋白 H4 定点 SUMO 化的全化学合成，以生成均一修饰的单核小体。这些单核小体被用作组蛋白 H2B 特异性泛素连接酶 Rad6 和 Bre1 的生化测定中的底物，结果表明 SUMO 强烈抑制了 H2B 的泛素化。这种 SUMO 和泛素之间的新型负生化串扰也被证实存在于人类细胞中。
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