Unraveling quiescence-specific repressive chromatin domains

Curr Genet. 2019 Oct;65(5):1145-1151. doi: 10.1007/s00294-019-00985-9. Epub 2019 May 4.

Abstract

Quiescence is a highly conserved inactive life stage in which the cell reversibly exits the cell cycle in response to external cues. Quiescence is essential for diverse processes such as the maintenance of adult stem cell stores, stress resistance, and longevity, and its misregulation has been implicated in cancer. Although the non-cycling nature of quiescent cells has made obtaining sufficient quantities of quiescent cells for study difficult, the development of a Saccharomyces cerevisiae model of quiescence has recently enabled detailed investigation into mechanisms underlying the quiescent state. Like their metazoan counterparts, quiescent budding yeast exhibit widespread transcriptional silencing and dramatic chromatin condensation. We have recently found that the structural maintenance of chromosomes (SMC) complex condensin binds throughout the quiescent budding yeast genome and induces the formation of large chromatin loop domains. In the absence of condensin, quiescent cell chromatin is decondensed and transcription is de-repressed. Here, we briefly discuss our findings in the larger context of the genome organization field.

Keywords: CIDs; Chromatin compaction; Cohesin; Condensin; Micro-C XL; Quiescence; TADs.

Publication types

  • Review

MeSH terms

  • Adenosine Triphosphatases / metabolism
  • Cell Cycle*
  • Chromatin / chemistry
  • Chromatin / genetics*
  • Chromatin / metabolism*
  • Chromatin Assembly and Disassembly / genetics
  • DNA-Binding Proteins / metabolism
  • Gene Expression Regulation
  • Genome-Wide Association Study
  • Multiprotein Complexes / metabolism
  • Resting Phase, Cell Cycle*
  • Saccharomyces cerevisiae / physiology
  • Saccharomyces cerevisiae Proteins / chemistry
  • Saccharomyces cerevisiae Proteins / genetics
  • Saccharomyces cerevisiae Proteins / metabolism
  • Transcription, Genetic

Substances

  • Chromatin
  • DNA-Binding Proteins
  • Multiprotein Complexes
  • Saccharomyces cerevisiae Proteins
  • condensin complexes
  • Adenosine Triphosphatases