Tricorn Protease in Bacteria: Characterization of the Enzyme from Streptomyces coelicolor
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Noriko Tamura
Abstract
Tricorn protease is believed to act downstream of the proteasome, or of other ATPdependent proteases, cleaving the oligopeptides (mostly 6 to 12 residues) released by them into small peptides (2 to 4 residues), before an array of aminopeptidases finally converts them into free amino acids. Hitherto, the occurrence of Tricorn protease seemed to be limited to some archaea, but genes encoding Tricorn homologs have now been found in several bacterial genomes. Among them is Streptomyces coelicolor A3(2), which has, in fact, two Tricornlike genes, ScC77.16c and ScE87.19. The proteins encoded by them (TRIScC77 and TRIScE87) are very similar in their PDZ and TSP domains, but rather divergent in their βpropeller domains. We have expressed one of them, TRIScC77, in E. coli and characterized the recombinant protein structurally and functionally. TRIScC77 forms a homohexameric complex of approximately 700 kDa, both in E. coli and in S. coelicolor, with enzymatic properties very similar to the complex from the archaeon Thermoplasma acidophilum. Thefact that Tricorn like proteins exist not only in thermoacidophiles, but also in bacteria inhabiting radically different environments, rules out the possibility that Tricorn protease is an adaptive element that helps to meet the challenges of an extreme habitat.
Copyright © 2001 by Walter de Gruyter GmbH & Co. KG
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- Highlight: Fluorescence Correlation Spectroscopy
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- Fluorescence Correlation Spectroscopy as a Tool to Investigate Single Molecule Probe Dynamics in Thin Polymer Films
- Ligand-Receptor Interactions in the Membrane of Cultured Cells Monitored by Fluorescence Correlation Spectroscopy
- Fluorescence Fluctuation Analysis for the Study of Interactions between Oligonucleotides and Polycationic Polymers
- Determination of the Net Exchange Rate of Tubulin Dimer in Steady-State Microtubules by Fluorescence Correlation Spectroscopy
- UV-Fluorescence Correlation Spectroscopy of 2-Aminopurine
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- Involvement of Intracellular Ca2+in the Regulation of Bovine Leukemia Virus Expression
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