Nickel Resistance and Chromatin Condensation in
Saccharomyces cerevisiae Expressing a Maize High Mobility
Group I/Y Protein*
Céline
Forzani,
Clarisse
Loulergue,
Stéphane
Lobréaux,
Jean-François
Briat, and
Michel
Lebrun
From Biochimie et Physiologie Moléculaire des Plantes, CNRS
Unité Mixte de Recherche 5004, Université Montpellier 2, Institut National de la Recherche Agronomique, Ecole Nationale
Supérieure d'Agronomie, 2 place Viala,
F-34060 Montpellier Cedex 1, France
Expression of a maize cDNA encoding a high
mobility group (HMG) I/Y protein enables growth of transformed yeast on
a medium containing toxic nickel concentrations. No difference in the
nickel content was measured between yeast cells expressing either the empty vector or the ZmHMG I/Y2 cDNA. The ZmHMG
I/Y2 protein contains four AT hook motifs known to be involved in
binding to the minor groove of AT-rich DNA regions. HMG I/Y proteins
may act as architectural elements modifying chromatin structure.
Indeed, a ZmHMG I/Y2-green fluorescent protein fusion protein was
observed in yeast nuclei. Nickel toxicity has been suggested to occur
through an epigenetic mechanism related to chromatin condensation and
DNA methylation, leading to the silencing of neighboring genes.
Therefore, the ZmHMG I/Y2 protein could prevent nickel toxicity by
interfering with chromatin structure. Yeast cell growth in the presence
of nickel and yeast cells expressing the ZmHMG I/Y2
cDNA increased telomeric URA3 gene silencing.
Furthermore, ZmHMG I/Y2 restored a wild-type level of nickel
sensitivity to the yeast
rpd3 mutant. Therefore, nickel
resistance of yeast cells expressing the ZmHMG I/Y2
cDNA is likely achieved by chromatin structure modification, restricting nickel accessibility to DNA.
*
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1734 solely to indicate this fact.
The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AF291748.