N- and C-terminal domains determine differential nucleosomal binding geometry and affinity of linker histone isotypes H1(0) and H1c.

@article{Vyas2012NAC,
  title={N- and C-terminal domains determine differential nucleosomal binding geometry and affinity of linker histone isotypes H1(0) and H1c.},
  author={Payal Vyas and David T. Brown},
  journal={The Journal of biological chemistry},
  year={2012},
  volume={287 15},
  pages={11778-87}
}
Eukaryotic linker or H1 histones modulate DNA compaction and gene expression in vivo. In mammals, these proteins exist as multiple isotypes with distinct properties, suggesting a functional significance to the heterogeneity. Linker histones typically have a tripartite structure composed of a conserved central globular domain flanked by a highly variable short N-terminal domain and a longer highly basic C-terminal domain. We hypothesized that the variable terminal domains of individual subtypes… CONTINUE READING

From This Paper

Figures, tables, and topics from this paper.

Citations

Publications citing this paper.
Showing 1-10 of 20 extracted citations

References

Publications referenced by this paper.
Showing 1-10 of 55 references

Evidence for a common mode of transcription factor interaction with chromatin as revealed by improved quantitative fluorescence recovery after photobleaching

F. Mueller, P. Wach, J. G. McNally
Biophys J • 2008
View 1 Excerpt

Similar Papers

Loading similar papers…