Journal
CROATICA CHEMICA ACTA
Volume 89, Issue 2, Pages -Publisher
CROATIAN CHEMICAL SOC
DOI: 10.5562/cca2806
Keywords
histone; nucleosome; chromatin; protein co-expression
Categories
Funding
- Gene Center
- BioSysNet
- ERC-smallRNAhet [309584]
- European Union Seventh Framework Programme (FP7) [291823]
- NEWFELPRO project [26]
- European Research Council (ERC) [309584] Funding Source: European Research Council (ERC)
Ask authors/readers for more resources
Functional and structural studies of histone-chaperone complexes, nucleosome modifications, their interactions with remodelers and regulatory proteins rely on obtaining recombinant histones from bacteria. In the present study, we show that co-expression of Xenopus laevis histone pairs leads to production of soluble H2AH2B heterodimer and (H3H4)2 heterotetramer. The soluble histone complexes are purified by simple chromatographic techniques. Obtained H2AH2B dimer and H3H4 tetramer are proficient in histone chaperone binding and histone octamer and nucleosome formation. Our optimized protocol enables rapid purification of multiple soluble histone variants with a remarkable high yield and simplifies histone octamer preparation. We expect that this simple approach will contribute to the histone chaperone and chromatin research.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available