Finding the end: recruitment of telomerase to telomeres

Nat Rev Mol Cell Biol. 2013 Feb;14(2):69-82. doi: 10.1038/nrm3505. Epub 2013 Jan 9.

Abstract

Telomeres, the ends of linear eukaryotic chromosomes, are characterized by the presence of multiple repeats of a short DNA sequence. This telomeric DNA is protected from illicit repair by telomere-associated proteins, which in mammals form the shelterin complex. Replicative polymerases are unable to synthesize DNA at the extreme ends of chromosomes, but in unicellular eukaryotes such as yeast and in mammalian germ cells and stem cells, telomere length is maintained by a ribonucleoprotein enzyme known as telomerase. Recent work has provided insights into the mechanisms of telomerase recruitment to telomeres, highlighting the contribution of telomere-associated proteins, including TPP1 in humans, Ccq1 in Schizosaccharomyces pombe and Cdc13 and Ku70-Ku80 in Saccharomyces cerevisiae.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Chromosomes / chemistry*
  • Chromosomes / metabolism
  • Humans
  • Models, Biological
  • Models, Molecular
  • Protein Binding / physiology
  • Saccharomyces cerevisiae / genetics
  • Saccharomyces cerevisiae / metabolism
  • Schizosaccharomyces / genetics
  • Schizosaccharomyces / metabolism
  • Shelterin Complex
  • Telomerase / metabolism*
  • Telomere / chemistry
  • Telomere / genetics
  • Telomere / metabolism*
  • Telomere-Binding Proteins

Substances

  • ACD protein, human
  • Shelterin Complex
  • Telomere-Binding Proteins
  • Telomerase