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          Institute: MPI für Biochemie     Collection: Structural Biology (W. Baumeister)     Display Documents

ID: 318782.0, MPI für Biochemie / Structural Biology (W. Baumeister)
Tricorn protease in bacteria: Characterization of the enzyme from Streptomyces coelicolor
Authors:Tamura, N.; Pfeifer, G.; Baumeister, W.; Tamura, T.
Date of Publication (YYYY-MM-DD):2001
Title of Journal:Biological Chemistry
Journal Abbrev.:Biol. Chem
Issue / Number:3
Start Page:449
End Page:458
Audience:Not Specified
Abstract / Description:Tricorn protease is believed to act downstream of the proteasome, or of other ATP-dependent 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 Tricorn-like genes, ScC77,16c and ScE87.19. The proteins encoded by them (TRI-ScC77 and TRI-ScE87) are very similar in their PDZ and TSP domains, but rather divergent in their beta -propeller domains. We have expressed one of them, TRI-ScC77, in E, coli and characterized the recombinant protein structurally and functionally. TRI-ScC77 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. The fact 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. [References: 32]
Free Keywords:Eubacteria; Streptomyces coelicolor; Tricorn protease.; Self-compartmentalizing proteases; Thermoplasma-acidophilum; Processive degradation; Escherichia-coli; Proteins; Sequence; System; Identification; Residues; Products.; Biochemistry & Biophysics in Current Contents(R)/Life Sciences.
External Publication Status:published
Document Type:Article
Communicated by:Anton Hillebrand
Affiliations:MPI für Biochemie/Structural Biology (W. Baumeister)/
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