Common Features of the Pericentromere and Nucleolus

Genes (Basel). 2019 Dec 10;10(12):1029. doi: 10.3390/genes10121029.

Abstract

Both the pericentromere and the nucleolus have unique characteristics that distinguish them amongst the rest of genome. Looping of pericentromeric DNA, due to structural maintenance of chromosome (SMC) proteins condensin and cohesin, drives its ability to maintain tension during metaphase. Similar loops are formed via condensin and cohesin in nucleolar ribosomal DNA (rDNA). Condensin and cohesin are also concentrated in transfer RNA (tRNA) genes, genes which may be located within the pericentromere as well as tethered to the nucleolus. Replication fork stalling, as well as downstream consequences such as genomic recombination, are characteristic of both the pericentromere and rDNA. Furthermore, emerging evidence suggests that the pericentromere may function as a liquid-liquid phase separated domain, similar to the nucleolus. We therefore propose that the pericentromere and nucleolus, in part due to their enrichment of SMC proteins and others, contain similar domains that drive important cellular activities such as segregation, stability, and repair.

Keywords: cohesin; condensin; nucleolus; pericentromere; rDNA.

Publication types

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

MeSH terms

  • Adenosine Triphosphatases
  • Cell Cycle Proteins
  • Cell Nucleolus / genetics*
  • Cell Nucleolus / metabolism
  • Cell Nucleolus / physiology*
  • Centromere / metabolism
  • Centromere / physiology*
  • Chromosomal Proteins, Non-Histone
  • Chromosome Segregation
  • Chromosomes / physiology
  • Cohesins
  • DNA-Binding Proteins
  • Mitosis
  • Multiprotein Complexes
  • Nucleolus Organizer Region / metabolism
  • Nucleolus Organizer Region / physiology
  • Saccharomyces cerevisiae / genetics
  • Saccharomyces cerevisiae Proteins / genetics

Substances

  • Cell Cycle Proteins
  • Chromosomal Proteins, Non-Histone
  • DNA-Binding Proteins
  • Multiprotein Complexes
  • Saccharomyces cerevisiae Proteins
  • condensin complexes
  • Adenosine Triphosphatases