ArticleMethods in enzymology2016
Rapid Semisynthesis of Acetylated and Sumoylated Histone Analogs.
Article in Methods in enzymology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 8 citations in OpenAlex.
- Article
- The semisynthesis of site-specifically modified histones and histone-based probes of chromatin-modifying enzymes.Methods (San Diego, Calif.) · 2023Article
- Preparation of Recombinant Histones and Widom 601 DNA for Reconstitution of Nucleosome Core Particles.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Nucleosome Core Particle Reconstitution with Recombinant Histones and Widom 601 DNA.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Strategies for Generating Modified Nucleosomes: Applications within Structural Biology Studies.ACS chemical biology · 2019Review
- A Highly Efficient Synthesis of Polyubiquitin Chains.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2018Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The density and diversity of posttranslational modifications (PTMs) observed in histone proteins typically limit their purification to homogeneity from biological sources. Access to quantities of uniformly modified histones is, however, critical for investigating the downstream effects of histone PTMs on chromatin-templated processes. Therefore, a number of semisynthetic methodologies have been developed to generate histones bearing precisely defined PTMs or close analogs thereof. In this chapter, we present two optimized and rapid strategies for generating functional analogs of site-specifically acetylated and sumoylated histones. First, we describe a convergent strategy to site-specifically attach the small ubiquitin-like modifier-3 (SUMO-3) protein to the site of Lys12 in histone H4 by means of a disulfide linkage. We then describe the generation of thialysine analogs of histone H3 acetylated at Lys14 or Lys56, using thiol-ene coupling chemistry. Both strategies afford multimilligram quantities of uniformly modified histones that are easily incorporated into mononucleosomes and nucleosome arrays for biophysical and biochemical investigations. These methods are readily extendable to any desired sites in the four core nucleosomal histones and their variant forms.
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