Hpz1 modulates the G1-S transition in fission yeast

PLoS One. 2012;7(9):e44539. doi: 10.1371/journal.pone.0044539. Epub 2012 Sep 6.

Abstract

Here we characterize a novel protein in S. pombe. It has a high degree of homology with the Zn-finger domain of the human Poly(ADP-ribose) polymerase (PARP). Surprisingly, the gene for this protein is, in many fungi, fused with and in the same reading frame as that encoding Rad3, the homologue of the human ATR checkpoint protein. We name the protein Hpz1 (Homologue of PARP-type Zn-finger). Hpz1 does not possess PARP activity, but is important for resistance to ultraviolet light in the G1 phase and to treatment with hydroxyurea, a drug that arrests DNA replication forks in the S phase. However, we find no evidence of a checkpoint function of Hpz1. Furthermore, absence of Hpz1 results in an advancement of S-phase entry after a G1 arrest as well as earlier recovery from a hydroxyurea block. The hpz1 gene is expressed mainly in the G1 phase and Hpz1 is localized to the nucleus. We conclude that Hpz1 regulates the initiation of the S phase and may cooperate with Rad3 in this function.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Cell Nucleus / metabolism
  • G1 Phase*
  • Humans
  • Molecular Sequence Data
  • S Phase*
  • Schizosaccharomyces / cytology
  • Schizosaccharomyces / metabolism*
  • Schizosaccharomyces pombe Proteins / chemistry
  • Schizosaccharomyces pombe Proteins / metabolism
  • Schizosaccharomyces pombe Proteins / physiology*
  • Sequence Homology, Amino Acid

Substances

  • Schizosaccharomyces pombe Proteins

Grants and funding

This work received funding from The Norwegian Cancer Society (www.kreftforeningen.no), from The Research Council of Norway (www.forskningsradet.no), and from the South-Eastern Norway Regional Health Authority (www.helse-sorost.no). The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.