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Journal of Bacteriology, January 2001, p. 716-724, Vol. 183, No. 2
0021-9193/01/$04.00+0 DOI: 10.1128/JB.183.2.716-724.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.
Key Role for Sulfur in Peptide Metabolism and in Regulation
of Three Hydrogenases in the Hyperthermophilic Archaeon
Pyrococcus furiosus
Michael W. W.
Adams,1,*
James F.
Holden,1
Angeli Lal
Menon,1
Gerrit J.
Schut,1
Amy M.
Grunden,1,
Chun
Hou,2
Andrea M.
Hutchins,1
Francis E.
Jenney Jr.,1
Chulhwan
Kim,1
Kesen
Ma,1,
Guangliang
Pan,1
Roopali
Roy,1
Rajat
Sapra,1
Sherry V.
Story,1 and
Marc F. J. M.
Verhagen1,§
Department of Biochemistry and Molecular
Biology, University of Georgia, Athens, Georgia
30602-7229,1 and Department of Biology,
Yunnan University, Kunming 650091, People's Republic of
China2
Received 7 June 2000/Accepted 25 October 2000
The hyperthermophilic archaeon Pyrococcus furiosus
grows optimally at 100°C by the fermentation of peptides and
carbohydrates. Growth of the organism was examined in media containing
either maltose, peptides (hydrolyzed casein), or both as the carbon
source(s), each with and without elemental sulfur (S0).
Growth rates were highest on media containing peptides and S0, with or without maltose. Growth did not occur on the
peptide medium without S0. S0 had no effect on
growth rates in the maltose medium in the absence of peptides.
Phenylacetate production rates (from phenylalanine fermentation) from
cells grown in the peptide medium containing S0 with or
without maltose were the same, suggesting that S0 is
required for peptide utilization. The activities of 14 of 21 enzymes
involved in or related to the fermentation pathways of P. furiosus were shown to be regulated under the five different growth conditions studied. The presence of S0 in the growth
media resulted in decreases in specific activities of two cytoplasmic
hydrogenases (I and II) and of a membrane-bound hydrogenase, each by an
order of magnitude. The primary S0-reducing enzyme in this
organism and the mechanism of the S0 dependence of peptide
metabolism are not known. This study provides the first evidence for a
highly regulated fermentation-based metabolism in P. furiosus and a significant regulatory role for elemental sulfur
or its metabolites.
*
Corresponding author. Mailing address: Department of
Biochemistry and Molecular Biology, Life Sciences Building, University of Georgia, Athens, GA 30602. Phone: (706) 542-2060. Fax: (706) 542-0229. E-mail: adams{at}bmb.uga.edu.

Present address: Department of Microbiology, North Carolina State
University, Raleigh, NC
27695.

Present address: Department of Biology, University of Waterloo,
Waterloo, Ontario, N2L 3G1
Canada.
§
Present address: Allergan Inc., Irvine, CA
92612.
Journal of Bacteriology, January 2001, p. 716-724, Vol. 183, No. 2
0021-9193/01/$04.00+0 DOI: 10.1128/JB.183.2.716-724.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.
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