A robust method for the purification and characterization of recombinant human histone H1 variants Journal Article
| Authors: | Osunsade, A.; Prescott, N. A.; Hebert, J. M.; Ray, D. M.; Jmeian, Y.; Lorenz, I. C.; David, Y. |
| Article Title: | A robust method for the purification and characterization of recombinant human histone H1 variants |
| Abstract: | Higher order compaction of the eukaryotic genome is key to the regulation of all DNA-templated processes, including transcription. This tightly controlled process involves the formation of mononucleosomes, the fundamental unit of chromatin, packaged into higher order architectures in an H1 linker histone-dependent process. While much work has been done to delineate the precise mechanism of this event in vitro and in vivo, major gaps still exist, primarily due to a lack of molecular tools. Specifically, there has never been a successful purification and biochemical characterization of all human H1 variants. Here we present a robust method to purify H1 and illustrate its utility in the purification of all somatic variants and one germline variant. In addition, we performed a first ever side-by-side biochemical comparison, which revealed a gradient of nucleosome binding affinities and compaction capabilities. These data provide new insight into H1 redundancy and lay the groundwork for the mechanistic investigation of disease-driving mutations. © 2018 American Chemical Society. |
| Journal Title: | Biochemistry |
| Volume: | 58 |
| Issue: | 3 |
| ISSN: | 0006-2960 |
| Publisher: | American Chemical Society |
| Date Published: | 2019-01-22 |
| Start Page: | 171 |
| End Page: | 176 |
| Language: | English |
| DOI: | 10.1021/acs.biochem.8b01060 |
| PROVIDER: | scopus |
| PUBMED: | 30585724 |
| PMCID: | PMC6541009 |
| DOI/URL: | |
| Notes: | Article -- Export Date: 1 February 2019 -- Source: Scopus |
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