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

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 chromosom...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Hauptverfasser: Poschke, Heiko (VerfasserIn) , Dees, Martina (VerfasserIn) , Kaderali, Lars (VerfasserIn) , Luke, Brian (VerfasserIn)
Dokumenttyp: Article (Journal)
Sprache:Englisch
Veröffentlicht: September 20, 2012
In: PLoS Genetics
Year: 2012, Jahrgang: 8, Heft: 9
ISSN:1553-7404
DOI:10.1371/journal.pgen.1002960
Online-Zugang:Verlag, kostenfrei, Volltext: http://dx.doi.org/10.1371/journal.pgen.1002960
Verlag, kostenfrei, Volltext: http://journals.plos.org/plosgenetics/article?id=10.1371/journal.pgen.1002960
Volltext
Verfasserangaben:Heiko Poschke, Martina Dees, Michael Chang, Sandeep Amberkar, Lars Kaderali, Rodney Rothstein, Brian Luke
Beschreibung
Zusammenfassung: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.
Beschreibung:Gesehen am 24.08.2018
Beschreibung:Online Resource
ISSN:1553-7404
DOI:10.1371/journal.pgen.1002960