The zinc finger protein Gsf1 regulates Gsf2-dependent flocculation in fission yeast

Tomohiko Matsuzawa, Youko Kageyama, Kazuyoshi Ooishi, Makoto Kawamukai, Kaoru Takegawa

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8 Citations (Scopus)


Fission yeast flocculates nonsexually by induction of the flocculin encoded by gsf2+ which is controlled by the positive regulator Mbx2. Here, we report a novel gene designated gsf1+ found to be a negative regulator of nonsexual flocculation. We identified gsf1+ as a multicopy suppressor of a sam2 mutation, which caused growth sensitivity to Ca2+ and also found a nonsense mutation in gsf1+ in a previously isolated gsf1 mutant. The gsf1+ gene encodes a 547-aa protein containing a Zn(2)-Cys(6) binuclear cluster-type zinc finger motif. The Gsf1 protein localized in the nucleus, consistent with a role as a transcription factor. Deletion of gsf1+ resulted in nonsexual flocculation inducible by CaCl2, which was suppressed by the addition of EDTA or galactose. Both gsf2+ and mbx2+ were highly expressed in the gsf1 mutant. gsf1{increment} gsf2{increment} and gsf1{increment} mbx2{increment} double mutants did not flocculate, suggesting that gsf1+ is an upstream regulator. In addition, the gsf1 mutant was sensitive to CaCl2, KCl, HU, and TBZ, consistent with the possibility that gsf1+ plays a role in functions unrelated to flocculation. Taken together, these results suggest that nonsexual flocculation in fission yeast is negatively controlled by Gsf1, which controls expression of mbx2+ and gsf2+.

Original languageEnglish
Pages (from-to)259-266
Number of pages8
JournalFEMS Yeast Research
Issue number3
Publication statusPublished - May 2013

All Science Journal Classification (ASJC) codes

  • Microbiology
  • Applied Microbiology and Biotechnology


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