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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MSK Authors
  1. Jakob M Hebert
    2 Hebert
  2. Devin Mary Ray
    3 Ray