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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,dagger Chun Hou,2 Andrea M. Hutchins,1 Francis E. Jenney Jr.,1 Chulhwan Kim,1 Kesen Ma,1,Dagger 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.

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

Dagger 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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Copyright © 2001 by the American Society for Microbiology. All rights reserved.