Targeting the Nucleosome Acidic Patch by Viral Proteins: Two Birds with One Stone?

The past decade illuminated the H2A-H2B acidic patch as a cornerstone for both nucleosome recognition and chromatin structure regulation. Higher-order folding of chromatin arrays is mediated by interactions of histone H4 tail with an adjacent nucleosome acidic patch. The past decade illuminated the H2A-H2B acidic patch as a cornerstone for both nucleosome recognition and chromatin structure regulation. Higher-order folding of chromatin arrays is mediated by interactions of histone H4 tail with an adjacent nucleosome acidic patch. Dynamic chromatin folding ensures a proper regulation of nuclear functions fundamental to cellular homeostasis. Many cellular factors have been shown to act on chromatin by tethering nucleosomes via an arginine anchor binding to the acidic patch. This tethering mechanism has also been described for several viral proteins. In this minireview, we will discuss the structural basis for acidic patch engagement by viral proteins and the implications during respective viral infections. We will also discuss a model in which acidic patch occupancy by these non-self viral proteins alters the local chromatin state by preventing H4 tail-mediated higher-order chromatin folding.

Automated summary

The H2A-H2B acidic patch has been identified as a key element for nucleosome recognition and chromatin structure regulation. The folding of chromatin arrays relies on the interaction between the histone H4 tail and the adjacent nucleosome acidic patch. Cellular factors and viral proteins have been found to bind to the acidic patch, influencing the chromatin state and potentially affecting viral infections.