Fission Yeast Pot1 and RecQ Helicase Are Required for Efficient Chromosome Segregation

Author:

Takahashi Katsunori1234,Imano Ryota1234,Kibe Tatsuya1234,Seimiya Hiroyuki1234,Muramatsu Yukiko1234,Kawabata Naoki1234,Tanaka Genki1234,Matsumoto Yoshitake1234,Hiromoto Taisuke1234,Koizumi Yuka1234,Nakazawa Norihiko1234,Yanagida Mitsuhiro1234,Yukawa Masashi1234,Tsuchiya Eiko1234,Ueno Masaru1234

Affiliation:

1. Department of Molecular Biotechnology, Graduate School of Advanced Sciences of Matter, Hiroshima University, 1-3-1 Kagamiyama, Higashi-Hiroshima 739-8530, Japan

2. Department of Chemistry, Shizuoka University, 836 Oya, Shizuoka 422-8529, Japan

3. Division of Molecular Biotherapy, Cancer Chemotherapy Center, Japanese Foundation for Cancer Research, 3-8-31 Ariake, Koto-Ku, Tokyo 135-8550, Japan

4. Graduate School of Biostudies, Kyoto University, Yoshida-Honmachi, Sakyo-Ku, Kyoto 606-8501, Japan

Abstract

ABSTRACT Pot1 is a single-stranded telomere-binding protein that is conserved from fission yeast to mammals. Deletion of Schizosaccharomyces 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 a pot1Δ rqh1-hd (helicase-dead) double mutant maintains telomeres that are dependent on Rad51-mediated homologous recombination. Interestingly, the pot1Δ 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 the pot1Δ 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 of S. pombe Pot1 and Rqh1 may be conserved in their respective human counterparts POT1 and WRN.

Publisher

American Society for Microbiology

Subject

Cell Biology,Molecular Biology

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