Fission Yeast Pot1 and RecQ Helicase Are Required for Efficient Chromosome Segregation
Author(s) -
Katsunori Takahashi,
Ryota Imano,
Tatsuya Kibe,
Hiroyuki Seimiya,
Yukiko Muramatsu,
Naoki Kawabata,
Genki Tanaka,
Yoshitake Matsumoto,
Taisuke Hiromoto,
Yuka Koizumi,
Norihiko Nakazawa,
Mitsuhiro Yanagida,
Masashi Yukawa,
Eiko Tsuchiya,
Masaru Ueno
Publication year - 2010
Publication title -
molecular and cellular biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.14
H-Index - 327
eISSN - 1067-8824
pISSN - 0270-7306
DOI - 10.1128/mcb.00613-10
Subject(s) - biology , recq helicase , schizosaccharomyces pombe , telomere binding protein , schizosaccharomyces , homologous recombination , telomere , genetics , chromosome segregation , microbiology and biotechnology , helicase , chromatid , mutant , genome instability , chromosome , dna , dna damage , gene , dna binding protein , rna , transcription factor
Pot1 is a single-stranded telomere-binding protein that is conserved from fission yeast to mammals. Deletion ofSchizosaccharomyces pombe pot1 + causes immediate telomere loss.S. pombe Rqh1 is a homolog of the human RecQ helicase WRN, which plays essential roles in the maintenance of genomic stability. Here, we demonstrate that apot1Δ rqh1-hd (helicase-dead) double mutant maintains telomeres that are dependent on Rad51-mediated homologous recombination. Interestingly, thepot1Δ rqh1-hd double mutant displays a “cut” (cell untimely torn) phenotype and is sensitive to the antimicrotubule drug thiabendazole (TBZ). Moreover, the chromosome ends of the double mutant do not enter the pulsed-field electrophoresis gel. These results suggest that the entangled chromosome ends in thepot1Δ rqh1-hd double mutant inhibit chromosome segregation, signifying that Pot1 and Rqh1 are required for efficient chromosome segregation. We also found that POT1 knockdown, WRN-deficient human cells are sensitive to the antimicrotubule drug vinblastine, implying that some of the functions ofS. pombe Pot1 and Rqh1 may be conserved in their respective human counterparts POT1 and WRN.
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