Rif2 promotes a telomere fold-back structure through Rpd3L recruitment in budding yeast

PLoS Genet. 2012 Sep;8(9):e1002960. doi: 10.1371/journal.pgen.1002960. Epub 2012 Sep 20.

Abstract

Using a genome-wide screening approach, we have established the genetic requirements for proper telomere structure in Saccharomyces cerevisiae. We uncovered 112 genes, many of which have not previously been implicated in telomere function, that are required to form a fold-back structure at chromosome ends. Among other biological processes, lysine deacetylation, through the Rpd3L, Rpd3S, and Hda1 complexes, emerged as being a critical regulator of telomere structure. The telomeric-bound protein, Rif2, was also found to promote a telomere fold-back through the recruitment of Rpd3L to telomeres. In the absence of Rpd3 function, telomeres have an increased susceptibility to nucleolytic degradation, telomere loss, and the initiation of premature senescence, suggesting that an Rpd3-mediated structure may have protective functions. Together these data reveal that multiple genetic pathways may directly or indirectly impinge on telomere structure, thus broadening the potential targets available to manipulate telomere function.

Publication types

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

MeSH terms

  • Acetylation
  • Chromatin / genetics
  • Chromosomes / genetics
  • Histone Deacetylases* / genetics
  • Histone Deacetylases* / metabolism
  • Lysine / genetics
  • Lysine / metabolism
  • Mutation
  • Saccharomyces cerevisiae / genetics*
  • Saccharomyces cerevisiae Proteins* / genetics
  • Saccharomyces cerevisiae Proteins* / metabolism
  • Telomere / genetics*
  • Telomere-Binding Proteins* / genetics
  • Telomere-Binding Proteins* / metabolism

Substances

  • Chromatin
  • RIF2 protein, S cerevisiae
  • Saccharomyces cerevisiae Proteins
  • Telomere-Binding Proteins
  • HDA1 protein, S cerevisiae
  • RPD3 protein, S cerevisiae
  • Histone Deacetylases
  • Lysine