The fission yeast gene encoding monothiol glutaredoxin 5 is regulated by nitrosative and osmotic stresses

Hong Gyum Kim, Eun Hee Park, Chang Jin Lim

Research output: Contribution to journalArticlepeer-review

9 Scopus citations

Abstract

Glutaredoxin (Grx) is a small, heat-stable redox protein acting as a multi-functional glutathione (GSH)-dependent disulfide oxidoreductase. We have cloned the monothiol Grx5 gene from the genomic DNA of the fission yeast Schizosaccharomyces pombe. It has 1,904 bp, with one intron, and encodes a putative protein of 146 amino acids with a molecular mass of 16.5 kDa. Recombinant Grx5 produced functional Grx in S. pombe cells. NO-generating sodium nitroprusside (SNP, 1.0 and 2.0 mM) and potassium chloride (KCl, 0.2 and 0.5 M) increased the synthesis of β-galactosidase from a Grx5-lacZ fusion gene, and transcription of Grx5 was also enhanced by SNP and KCl. Synthesis of β-galactosidase from the Grx5-lacZ fusion was lower in Pap1-negative TP108-3C cells than in wild type KP1 cells, and when Pap1 was overproduced in KP1 cells, the level of β-galactosidase increased. We also found that Pap1 is involved in the induction of Grx5 by SNP and KC1. S. pombe Grx5 may play a crucial role in responses to nitrosative and osmotic stresses.

Original languageEnglish (US)
Pages (from-to)43-50
Number of pages8
JournalMolecules and Cells
Volume20
Issue number1
StatePublished - Dec 1 2005

Keywords

  • Grx5-lacZ
  • Monothiol Glutaredoxin
  • Pap1
  • Regulation
  • S. pombe
  • Stress Response

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