BLM helicase complements disrupted type II telomere lengthening in telomerase-negative sgs1 yeast

Cancer Res. 2005 Jul 1;65(13):5520-2. doi: 10.1158/0008-5472.CAN-05-0632.

Abstract

Recombination-mediated pathways for telomere lengthening may be utilized in the absence of telomerase activity. The RecQ-like helicases, BLM and Sgs1, are implicated in recombination-mediated telomere lengthening in human cells and budding yeast, respectively. Here, we show that BLM expression rescues disrupted telomere lengthening in telomerase-negative sgs1 yeast. BLM helicase activity is required for this complementation, indicating BLM and Sgs1 resolve the same telomeric structures. These data support a conserved function for BLM and Sgs1 in recombination-mediated telomere lengthening.

Publication types

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

MeSH terms

  • Adenosine Triphosphatases / genetics
  • Adenosine Triphosphatases / metabolism
  • Adenosine Triphosphatases / physiology*
  • DNA Helicases / deficiency
  • DNA Helicases / genetics
  • DNA Helicases / metabolism
  • DNA Helicases / physiology*
  • Mutagenesis, Site-Directed
  • RecQ Helicases
  • Saccharomyces cerevisiae / enzymology*
  • Saccharomyces cerevisiae / genetics
  • Saccharomyces cerevisiae / ultrastructure
  • Saccharomyces cerevisiae Proteins / genetics
  • Saccharomyces cerevisiae Proteins / metabolism
  • Saccharomyces cerevisiae Proteins / physiology*
  • Telomerase / deficiency*
  • Telomere / genetics
  • Telomere / metabolism
  • Telomere / physiology*

Substances

  • Saccharomyces cerevisiae Proteins
  • Telomerase
  • Adenosine Triphosphatases
  • Bloom syndrome protein
  • SGS1 protein, S cerevisiae
  • DNA Helicases
  • RecQ Helicases