Abstract
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.
Dokumententyp: | Zeitschriftenartikel |
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Fakultät: | Chemie und Pharmazie > Department Biochemie |
Themengebiete: | 500 Naturwissenschaften und Mathematik > 540 Chemie |
URN: | urn:nbn:de:bvb:19-epub-38171-5 |
ISSN: | 0011-1643 |
Sprache: | Englisch |
Dokumenten ID: | 38171 |
Datum der Veröffentlichung auf Open Access LMU: | 04. Mai 2017, 13:11 |
Letzte Änderungen: | 04. Nov. 2020, 14:45 |