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Molecular and General Genetics MGG

, Volume 258, Issue 1–2, pp 139–147 | Cite as

Phosphoinositide-specific phospholipase C forms a complex with 14-3-3 proteins and is involved in expression of UV resistance in fission yeast

  • T. Andoh
  • T. Kato Jr
  • Y. Matsui
  • A. Toh-e
ORIGINAL PAPER

Abstract

The fission yeast plc1+ gene encodes phosphoinositide-specific phospholipase C. The two- hybrid interaction assay with plexA-plc1+ as a bait revealed that Plc1p interacted with the 14-3-3 proteins Rad24p and Rad25p. Formation of a complex containing Plc1p and Rad24p in vivo was confirmed by an immunological method. As predicted from the fact that rad24 null mutant cells are hypersensitive to UV irradiation, plc1 null mutant cells were almost as sensitive to UV irradiation as rad24 null mutant cells. In addition, deletion of rad24 in the plc1 null mutant cells did not enhance the UV sensitivity, indicating that plc1+ and rad24+ belong to the same epistasis group with respect to UV sensitivity. Whereas Rad24p has been reported to be involved in the DNA damage checkpoint pathway, the delay to mitosis after UV irradiation was not defective either in rad24 null mutant cells or in plc1 null mutant cells in our analysis. Thus, Plc1p is responsible for resistance to UV irradiation, but not for the DNA damage checkpoint pathway, in cooperation with 14-3-3 proteins.

Key Words Phospholipase C 14-3-3 proteins Rad24p and Rad25p UV 

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Copyright information

© Springer-Verlag Berlin Heidelberg 1998

Authors and Affiliations

  • T. Andoh
    • 1
  • T. Kato Jr
    • 2
  • Y. Matsui
    • 1
  • A. Toh-e
    • 1
  1. 1.Department of Biological Sciences, Graduate School of Science, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113, JapanJP
  2. 2.The Okayama Cell Switching Project, ERATO, JRDC, Pasteur Building 4F, 103-5 Tanaka Monzen-cho, Sakyo-ku, Kyoto 606, JapanJP

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