Studies of biochemical crosstalk in chromatin with semisynthetic histones
| Autor: | Champak Chatterjee, Esha Upadhyay, Calvin Jon Antolin Leonen |
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| Rok vydání: | 2018 |
| Předmět: |
Models
Molecular 0301 basic medicine SUMO protein 010402 general chemistry 01 natural sciences Biochemistry Article Analytical Chemistry Histones 03 medical and health sciences Ubiquitin Animals Humans Histone code Gene biology Chemistry Ubiquitination Sumoylation Semisynthesis Chromatin Nucleosomes 0104 chemical sciences Cell biology Histone Code Crosstalk (biology) 030104 developmental biology Histone Small Ubiquitin-Related Modifier Proteins biology.protein |
| Zdroj: | Current Opinion in Chemical Biology. 45:27-34 |
| ISSN: | 1367-5931 |
| Popis: | Reversible post-translational modifications of histone proteins in eukaryotic chromatin are closely tied to gene function and cellular development. Specific combinations of histone modifications, or marks, are implicated in distinct DNA-templated processes mediated by a range of chromatin-associated enzymes that install, erase and interpret the histone code. Mechanistic studies of the precise biochemical relationship between sets of marks and their effects on chromatin function are significantly complicated by the dynamic nature and heterogeneity of marks in cellular chromatin. Protein semisynthesis is a chemical technique that enables the piecewise assembly of uniformly and site-specifically modified histones in quantities sufficient for biophysical and biochemical analyses. Recent pioneering efforts in semisynthesis have yielded access to histones site-specifically modified by entire proteins, such as ubiquitin (Ub) and the small ubiquitin-like modifier (SUMO). Herein, we highlight key studies of biochemical crosstalk involving Ub and SUMO in chromatin that were enabled by histone semisynthesis. |
| Databáze: | OpenAIRE |
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