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. 1992 Apr;58(4):1134–1141. doi: 10.1128/aem.58.4.1134-1141.1992

Regulation of Proteolytic Activity in the Hyperthermophile Pyrococcus furiosus

Lesley J Snowden 1, Ilse I Blumentals 1, Robert M Kelly 1,*
PMCID: PMC195566  PMID: 16348684

Abstract

Pyrococcus furiosus was shown to grow on casein or peptides as the sole carbon, energy, and nitrogen sources, while maltose could be used as a carbon and energy source only if peptides were present in the medium. A mixture of all 20 single amino acids could not replace the peptide requirement. Specific intracellular proteolytic activity was induced under low casein or tryptone levels and was decreased by the addition of maltose to both peptide-limiting and peptide-rich media in batch and continuous cultures. In a peptide-limited chemostat, activity towards azocasein and MeO-Suc-Arg-Pro-Tyr-p-nitroanilide reached a maximum at a dilution rate of 0.28 h-1, while activity toward l-lysine-p-nitroanilide reached a maximum at 0.50 h-1. Under peptide-limiting conditions, levels of the 66-kDa protease (S66) were enhanced relative to those of other cell proteins. Preliminary evidence suggests that this protease is immunologically related to the eukaryotic multicatalytic proteinase complex (proteosome).

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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