Heterochromatin aggregation during DNA elimination in Tetrahymena is facilitated by a prion-like protein

J Cell Sci. 2017 Jan 15;130(2):480-489. doi: 10.1242/jcs.195503. Epub 2016 Dec 1.


Regulated aggregations of prion and prion-like proteins play physiological roles in various biological processes. However, their structural roles in the nucleus are poorly understood. Here, we show that the prion-like protein Jub6p is involved in the regulation of chromatin structure in the ciliated protozoan Tetrahymena thermophila Jub6p forms sodium dodecyl sulfate (SDS)-resistant aggregates when it is ectopically expressed in vegetative cells and binds to RNA in vitro Jub6p is a heterochromatin component and is important for the formation of heterochromatin bodies during the process of programmed DNA elimination. We suggest that RNA-protein aggregates formed by Jub6p are an essential architectural component for the assembly of heterochromatin bodies.

Keywords: DNA elimination; Heterochromatin; Heterochromatin body; Prion; Tetrahymena.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Biological Assay
  • DNA / metabolism*
  • Heterochromatin / metabolism*
  • Phosphorylation
  • Prions / metabolism*
  • Protein Aggregates*
  • Protein Binding
  • Protein Domains
  • Protozoan Proteins / chemistry
  • Protozoan Proteins / metabolism
  • RNA / metabolism
  • Tetrahymena thermophila / metabolism*


  • Heterochromatin
  • Prions
  • Protein Aggregates
  • Protozoan Proteins
  • RNA
  • DNA