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Homomultimeric protease in the hyperthermophilic bacterium Thermotoga maritima has structural and amino acid sequence homology to bacteriocins in mesophilic bacteria
Author(s) -
Hicks Paula M,
Rinker Kristina D,
Baker Joey R,
Kelly Robert M
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)01451-3
Subject(s) - thermotoga maritima , protease , bacteriocin , bacteria , biology , biochemistry , microbiology and biotechnology , mesophile , escherichia coli , enzyme , antimicrobial , genetics , gene
A novel homomultimeric protease (>669 kDa), based on 31 kDa subunits, was purified from cell extracts of the hyperthermophilic bacterium Thermotoga maritima . This protease exhibits activity toward chymotrypsin and trypsin substrates, optimally at 90°C and pH 7.1, and has a half‐life of 36 min at 95°C. Transmission electron microscopy established that the protease consists of a large globular assembly which appears circular from the front view. The function of this protease in T . maritima remains unclear, although putative homologs include a 29 kDa antigen from Mycobacterium tuberculosis and a 31 kDa monomer of a high molecular weight bacteriocin produced by Brevibacterium linens [Valdes‐Stauber, N. and Scherer, S. (1996) Appl. Environ. Microbiol. 62, 1283–1286]. The relationship of these mesophilic proteins to the T . maritima protease suggests that their antibacterial activity may involve elements of proteolysis, and raises the prospect for anti‐microbial ecological strategies in hyperthermophilic niches.