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PMID: 15994923 Published · ppublish English Journal Article Research Support, N.I.H., Extramural Research Support, U.S. Gov't, P.H.S.

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

Cancer research ·Vol. 65 ·No. 13 ·2005-07-01 ·Pages 5520-2

Lillard-Wetherell K, Combs KA, Groden J

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.

MeSH Terms
Adenosine Triphosphatases/genetics,metabolism,physiology DNA Helicases/deficiency,genetics,metabolism,physiology Mutagenesis, Site-Directed RecQ Helicases Saccharomyces cerevisiae/enzymology,genetics,ultrastructure Saccharomyces cerevisiae Proteins/genetics,metabolism,physiology Telomerase/deficiency Telomere/genetics,metabolism,physiology
Chemicals
Saccharomyces cerevisiae Proteins Telomerase Adenosine Triphosphatases Bloom syndrome protein SGS1 protein, S cerevisiae DNA Helicases RecQ Helicases
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Lillard-Wetherell Kate
Department of Molecular Genetics, Biochemistry and Microbiology, University of Cincinnati College of Medicine, Cincinnati, Ohio 45267-0524, USA.
Combs Kelly A
Groden Joanna
Article Info
Journal
Cancer research
Abbr.
Cancer Res
ISSN
0008-5472
Published
2005-07-01
Pages
5520-2
Language
English
Region
United States
NLM ID
2984705R
Subset
IM
Grants
NIEHS NIH HHS · P30-ES06096 · United States
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