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Title: Bioenergetic and physiological studies of hyperthermophilic archaea. Final report

Abstract

This project focuses on physiological and bioenergetic characteristics of two representative hyperthermophilic archaea: Thermococcus litoralis (T{sub opt} 88 C) and Pyrococcus furiosus (T{sub opt} 98 C). Both are obligately anaerobic heterotrophs which grow in the presence or absence of reducible sulfur compounds. T. litoralis was studied in relation to information previously developed for P. furiosus: effect of sulfur reduction on bioenergetics, preferred fermentation patterns, tungsten requirement, etc. A defined medium was developed for T. litoralis consisting of amino acids, vitamins and nucleotides. This serves as the basis for continuous culture studies probing metabolic response to media changes. P. furiosus and T. litoralis have also been found to produce a polysaccharide in the presence of maltose and yeast extract. The composition and chemical structure of this polysaccharide was investigated as well as the metabolic motivation for its production. A novel and, perhaps, primitive intracellular proteolytic complex (previously designated as protease S66) in P. furiosus was isolated and the gene encoding the subunit of the complex was cloned, sequenced and the protease expressed in active form in Eschericia coli. Among other issues, the role of this complex in protein turnover and stress response was examined in the context of this organism inmore » addition to comparing it to other complexes in eubacterial and eukaryotic cells. Biochemical characteristics of the protease have been measured in addition to examining other proteolytic species in P. furiosus.« less

Authors:
Publication Date:
Research Org.:
North Carolina State Univ., Dept. of Chemical Engineering, Raleigh, NC (United States)
Sponsoring Org.:
USDOE Office of Energy Research, Washington, DC (United States)
OSTI Identifier:
325744
Report Number(s):
DOE/ER/20113-1
ON: DE99002032; TRN: AHC29910%%52
DOE Contract Number:  
FG05-93ER20113
Resource Type:
Technical Report
Resource Relation:
Other Information: PBD: [1999]
Country of Publication:
United States
Language:
English
Subject:
55 BIOLOGY AND MEDICINE, BASIC STUDIES; PROGRESS REPORT; BACTERIA; CHEMICAL COMPOSITION; PHYSIOLOGY; PEPTIDE HYDROLASES; EXPERIMENTAL DATA

Citation Formats

Kelly, R M. Bioenergetic and physiological studies of hyperthermophilic archaea. Final report. United States: N. p., 1999. Web. doi:10.2172/325744.
Kelly, R M. Bioenergetic and physiological studies of hyperthermophilic archaea. Final report. United States. https://doi.org/10.2172/325744
Kelly, R M. 1999. "Bioenergetic and physiological studies of hyperthermophilic archaea. Final report". United States. https://doi.org/10.2172/325744. https://www.osti.gov/servlets/purl/325744.
@article{osti_325744,
title = {Bioenergetic and physiological studies of hyperthermophilic archaea. Final report},
author = {Kelly, R M},
abstractNote = {This project focuses on physiological and bioenergetic characteristics of two representative hyperthermophilic archaea: Thermococcus litoralis (T{sub opt} 88 C) and Pyrococcus furiosus (T{sub opt} 98 C). Both are obligately anaerobic heterotrophs which grow in the presence or absence of reducible sulfur compounds. T. litoralis was studied in relation to information previously developed for P. furiosus: effect of sulfur reduction on bioenergetics, preferred fermentation patterns, tungsten requirement, etc. A defined medium was developed for T. litoralis consisting of amino acids, vitamins and nucleotides. This serves as the basis for continuous culture studies probing metabolic response to media changes. P. furiosus and T. litoralis have also been found to produce a polysaccharide in the presence of maltose and yeast extract. The composition and chemical structure of this polysaccharide was investigated as well as the metabolic motivation for its production. A novel and, perhaps, primitive intracellular proteolytic complex (previously designated as protease S66) in P. furiosus was isolated and the gene encoding the subunit of the complex was cloned, sequenced and the protease expressed in active form in Eschericia coli. Among other issues, the role of this complex in protein turnover and stress response was examined in the context of this organism in addition to comparing it to other complexes in eubacterial and eukaryotic cells. Biochemical characteristics of the protease have been measured in addition to examining other proteolytic species in P. furiosus.},
doi = {10.2172/325744},
url = {https://www.osti.gov/biblio/325744}, journal = {},
number = ,
volume = ,
place = {United States},
year = {Mon Mar 01 00:00:00 EST 1999},
month = {Mon Mar 01 00:00:00 EST 1999}
}