Homomultimeric protease in the hyperthermophilic bacterium Thermotoga maritima has structural and amino acid sequence homology to bacteriocins in mesophilic bacteria

FEBS Letters

Hicks, Paula M¹  Baker, Joey R¹  Rinker, Kristina D¹  Kelly, Robert M¹ 

[1] Department of Chemical Engineering, North Carolina State University, Raleigh, NC 27695-7905, USA

关键词: Proteolysis;    Bacteriocin;    Thermotoga;    SPB;    sodium phosphate buffer;    PPB;    potassium phosphate buffer;    VKM;    N-carbobenzyloxy-valine-lysine-methionine;    MCA;    7-amino-4-methylcoumarin;    A-K;    alanine-lysine;    PAGE;    polyacrylamide gel electrophoresis;    SDS;    sodium dodecyl sulfate;    TCA;    trichloroacetic acid;    TEM;    transmission electron microscopy;   

DOI  :  10.1016/S0014-5793(98)01451-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown