Chromatin motion is constrained by association with nuclear compartments in human cells

Curr Biol. 2002 Mar 19;12(6):439-45. doi: 10.1016/s0960-9822(02)00695-4.

Abstract

Background: In comparison with many nuclear proteins, the movement of chromatin in nuclei appears to be generally constrained. These restrictions on motion are proposed to reflect the attachment of chromatin to immobile nuclear substructures.

Results: To gain insight into the regulation of chromosome dynamics by nuclear architecture, we have followed the movements of different sites in the human genome in living cells. Here, we show that loci at nucleoli or the nuclear periphery are significantly less mobile than other, more nucleoplasmic loci. Disruption of nucleoli increases the mobility of nucleolar-associated loci.

Conclusions: This is the first report of distinct nuclear substructures constraining the movements of chromatin. These constraints reflect the physical attachment of chromatin to nuclear compartments or steric impairment caused by local ultrastructure. Our data suggest a role for the nucleolus and nuclear periphery in maintaining the three-dimensional organization of chromatin in the human nucleus.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism
  • Cell Compartmentation
  • Cell Nucleolus / genetics
  • Cell Nucleolus / metabolism
  • Cell Nucleus / metabolism
  • Cell Nucleus / ultrastructure*
  • Cells, Cultured
  • Chromatin / metabolism*
  • Chromatin / ultrastructure
  • Escherichia coli Proteins*
  • Fibroblasts
  • Genome, Human
  • Green Fluorescent Proteins
  • Humans
  • In Situ Hybridization, Fluorescence
  • Lac Repressors
  • Luminescent Proteins / genetics
  • Luminescent Proteins / metabolism
  • Recombinant Fusion Proteins / genetics
  • Recombinant Fusion Proteins / metabolism
  • Repressor Proteins / genetics
  • Repressor Proteins / metabolism

Substances

  • Bacterial Proteins
  • Chromatin
  • Escherichia coli Proteins
  • Lac Repressors
  • Luminescent Proteins
  • Recombinant Fusion Proteins
  • Repressor Proteins
  • Green Fluorescent Proteins