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Extreme arsenic resistance by the acidophilic archaeon Ferroplasma
acidarmanus Fer1
Craig Baker-Austin1,6, Mark Dopson1,2, Margaret
Wexler1, R. Gary Sawers3, Ann Stemmler4,
Barry P. Rosen4, and Philip L. Bond1,5,7
1School of Biological Sciences, University of East Anglia,
Norwich NR4 7TJ, UK
2Molecular
Biology, Umeå University, SE-901 87 Umeå, Sweden
3Department of Molecular Biology, John Innes Centre, Norwich
NR4 7UH, UK
4Department of Biochemistry and Molecular Biology, Wayne state
University, School of Medicine, Detroit, MI 48210, USA
5Centre for Ecology, Evolution and Conservation, University
of East Anglia, Norwich NR4 7TJ, UK
6Savannah River Ecology Laboratory, The University of Georgia,
Aiken, SC 29802, USA
7Advanced Wastewater Management Centre, University of Queensland,
Brisbane 4072 QLD, Australia
Abstract
Ferroplasma
acidarmanus Fer1 is an arsenic-hypertolerant acidophilic archaeon
isolated from the Iron Mountain mine, California; a site characterized
by heavy metals contamination. The presence of up to 10 g arsenate per
litre [As(V); 133 mM] did not significantly reduce growth yields, whereas
between 5 and 10 g arsenite per litre [As(III); 67133 mM] significantly
reduced the yield. Previous bioinformatic analysis indicates that F.
acidarmanus Fer1 has only two predicted genes involved in arsenic
resistance and lacks a recognizable gene for an arsenate reductase. Biochemical
analysis suggests that F. acidarmanus Fer1 does not
reduce arsenate indicating that F. acidarmanus Fer1
has an alternative resistance mechanism to arsenate other than reduction
to arsenite and efflux. Primer extension analysis of the putative ars
transcriptional regulator (arsR) and efflux pump (arsB)
demonstrated that these genes are co-transcribed, and expressed in response
to arsenite, but not arsenate. Two-dimensional polyacrylamide gel electrophoresis
analysis of F. acidarmanus Fer1 cells exposed to arsenite
revealed enhanced expression of proteins associated with protein refolding,
including the thermosome Group II HSP60 family chaperonin and
HSP70 DnaK type heat shock proteins. This report represents the first
molecular and proteomic study of arsenic resistance in an acidophilic
archaeon.
Keywords
Ferroplasma, Arsenic resistance, Arsenite, Proteomics, Primer extension
SREL Reprint #3036
Baker-Austin,
C., M. Dopson, M. Wexler, R. G. Sawers, A. Stemmler, B. P. Rosen, and
P. L. Bond. 2007. Extreme
arsenic resistance by the acidophilic archaeon Ferroplasma acidarmanus
Fer1. Extremophiles (2007)11:425-434.
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