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Iron homeostasis in the fission yeast Schizosaccharomyces pombe

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Abstract

Schizosaccharomyces pombe has acquisition processes for iron, an essential nutrient. One pathway consists to produce, excrete, and capture siderophore–iron complexes. A second pathway requires enzymatic reduction of ferric iron at the cell surface prior to uptake by a permease–oxidase complex. Genes encoding proteins involved in iron assimilation are transcriptionally regulated as a function of iron availability. Under high iron conditions, the GATA-type regulator Fep1 represses the expression of iron uptake genes. The repressor function of Fep1 requires the presence of the Tup11 or Tup12 transcriptional co-repressor. Under low iron conditions, two regulatory mechanisms occur. First, the iron transport genes are highly induced. Second, there is a transcription factor cascade implicating the heteromeric CCAAT-binding complex that turns off a set of genes encoding iron-utilizing proteins, presumably to avoid a futile expenditure of energy in producing iron-using proteins that lack the necessary cofactor to function. Thus, collectively, these regulatory responses to variations in iron concentrations ensure that iron is present within cells for essential biochemical reactions, yet prevent the accumulation of iron or iron-using proteins to deleterious levels.

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Notes

  1. B. Pelletier, A. Mercier, and S. Labbé, unpublished data.

  2. M. Durand, B. Pelletier, M. Bisaillon, and S. Labbé, unpublished data.

  3. A. Mercier and S. Labbé, unpublished data.

  4. In this review, we used the nomenclature for Schizosaccharomyces pombe and Saccharomyces cerevisiae genes and proteins. S. pombe wild-type genes are in regular text, italicized, with a superscripted “+” at the end (e.g., fep1 +). S. cerevisiae wild-type genes are capitalized and italicized (e.g., AFT1). S. pombe and S. cerevisiae protein nomenclature is the same and is indicated with a capital letter at the beginning followed by regular letters (e.g., Aft1, Fep1).

Abbreviations

AD:

Activation domain

K d,app :

Apparent dissociation constant

bp:

Base pair(s)

BPS:

Bathophenanthrolinedisulfonic acid

DBD:

DNA-binding domain

Dip:

2,2’ Dipyridyl

Fep1:

Fe protein 1

ORF:

Open reading frame

ZF1:

N-terminal zinc finger

ZF2:

C-terminal zinc finger

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Acknowledgments

We are grateful to Éric Massé for critically reading the manuscript and for his valuable comments. We thank our colleagues of the Labbé laboratory for their contributions. Research in the Labbé laboratory on iron homeostasis in fission yeast is funded by the Natural Sciences and Engineering Research Council of Canada (NSERC Grant 238238-01). A. M. and B. P. are recipients of studentships from the Natural Sciences and Engineering Research Council of Canada (NSERC) and the Fonds de la Recherche en Santé du Québec (FRSQ), respectively. S. L. is a Scholar from the FRSQ.

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  1. Département de Biochimie, Faculté de médecine, Université de Sherbrooke, 3001 12e Ave Nord, Sherbrooke, QC, Canada, J1H 5N4

    Simon Labbé, Benoit Pelletier & Alexandre Mercier

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  1. Simon Labbé
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Correspondence to Simon Labbé.

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Labbé, S., Pelletier, B. & Mercier, A. Iron homeostasis in the fission yeast Schizosaccharomyces pombe . Biometals 20, 523–537 (2007). https://doi.org/10.1007/s10534-006-9056-5

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