AI Article Synopsis
- Higher order folding of chromatin is influenced by the interactions between the histone H4 N-terminal tails and neighboring nucleosomes, leading to chromatin compaction.
- Various proteins (like LANA, IL-33, RCC1, Sir3, and HMGN2) have been studied for their binding to nucleosomes, where they compete for the same binding site on the nucleosome's acidic patch due to similar interaction characteristics.
- The binding of these proteins can disrupt the normal folding process of chromatin by interfering with the H4 tails, resulting in the formation of alternative chromatin structures that may have different biological roles.
Article Abstract
Higher order folding of chromatin fibre is mediated by interactions of the histone H4 N-terminal tail domains with neighbouring nucleosomes. Mechanistically, the H4 tails of one nucleosome bind to the acidic patch region on the surface of adjacent nucleosomes, causing fibre compaction. The functionality of the chromatin fibre can be modified by proteins that interact with the nucleosome. The co-structures of five different proteins with the nucleosome (LANA, IL-33, RCC1, Sir3 and HMGN2) recently have been examined by experimental and computational studies. Interestingly, each of these proteins displays steric, ionic and hydrogen bond complementarity with the acidic patch, and therefore will compete with each other for binding to the nucleosome. We first review the molecular details of each interface, focusing on the key non-covalent interactions that stabilize the protein-acidic patch interactions. We then propose a model in which binding of proteins to the nucleosome disrupts interaction of the H4 tail domains with the acidic patch, preventing the intrinsic chromatin folding pathway and leading to assembly of alternative higher order chromatin structures with unique biological functions.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3627075 | PMC |
| http://dx.doi.org/10.1098/rsif.2012.1022 | DOI Listing |
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