| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 2030882 | Trends in Biochemical Sciences | 2013 | 4 Pages |
Abstract
Histones are among the most conserved proteins in eukaryotes: the structural constraints of the nucleosome pose a challenge to evolving novel function. Nevertheless, confined histone surfaces have diversified, allowing the modulation of basic chromatin function through specialized histone chaperones. Recent structures of three histone–chaperone complexes, DAXX, HJURP, and Scm3, exemplify a common parsimonious solution to the restricted evolutionary space of histone recognition by their cognate histone chaperones: the reutilization of existing themes in histone structural biology.
Related Topics
Life Sciences
Biochemistry, Genetics and Molecular Biology
Biochemistry
Authors
Simon J. Elsässer,