Dynamic fuzziness during linker histone action

Adv Exp Med Biol. 2012:725:15-26. doi: 10.1007/978-1-4614-0659-4_2.

Abstract

Linker histones are multi-domain nucleosome binding proteins that stabilize higher order chromatin structures and engage in specific protein-protein interactions. Here we emphasize the structural and functional properties of the linker histone C-terminal domain (CTD), focusing on its intrinsic disorder, interaction-induced secondary structure formation and dynamic fuzziness. We argue that the fuzziness inherent in the CTD is a primary molecular mechanism underlying linker histone function in the nucleus.

Publication types

  • Research Support, N.I.H., Extramural
  • Review

MeSH terms

  • Animals
  • Chromatin / metabolism*
  • Histones / chemistry*
  • Histones / metabolism*
  • Humans
  • Nucleosomes
  • Protein Binding
  • Proteins / chemistry*
  • Proteins / metabolism*

Substances

  • Chromatin
  • Histones
  • Nucleosomes
  • Proteins