Gene expression and activity analysis of the first thermophilic U32 peptidase
| Autor: | Mindaugas Valius, Donaldas Chitavichius, Marija Ger, Algirdas Kaupinis, Nomeda Kuisiene, Andrius Jasilionis |
|---|---|
| Rok vydání: | 2012 |
| Předmět: |
QH301-705.5
Peptidase Gene geobacillus thermoleovorans General Biochemistry Genetics and Molecular Biology law.invention Microbiology geobacillus lituanicus law Gene expression medicine Biology (General) chemistry.chemical_classification General Immunology and Microbiology biology Constitutive expression Collagenolytic activity Thermophilic collagenase Geobacillus thermoleovorans Geobacillus lituanicus General Neuroscience Thermophile collagenolytic activity biology.organism_classification Hyperthermophile Enzyme Biochemistry chemistry Recombinant DNA Collagenase thermophilic collagenase General Agricultural and Biological Sciences constitutive expression Bacteria medicine.drug |
| Zdroj: | Central European journal of biology, Warsaw : Versita, 2012, Vol. 7, no. 4, p. 587-595 Open Life Sciences, Vol 7, Iss 4, Pp 587-595 (2012) |
| ISSN: | 2391-5412 1895-104X |
| DOI: | 10.2478/s11535-012-0047-y |
| Popis: | Peptidase family U32 is one of the few whose catalytic type and structure has not yet been described. It is generally accepted that U32 peptidases represent putative collagenases and contribute to the pathogenicity of some bacteria. Meanwhile, U32 peptidases are also found in nonpathogenic bacteria including thermophiles and hyperthermophiles. Here we report cloning of the U32.002 peptidase gene from thermophilic Geobacillus thermoleovorans DSM 15325 and demonstrate expression and characterization of the recombinant protein. It has been determined that U32.002 peptidase is constitutively expressed in the cells of thermophilic G. thermoleovorans DSM 15325. The recombinant oligomeric enzyme showed its activity only against heat-treated collagen. It was unable to degrade albumin, casein, elastin, gelatine and keratin. In contrast to this, the monomeric recombinant protein showed no activity at all. This paper is the first report about the thermophilic U32 peptidase. As the thermophilic bacteria are non-pathogenic, the role of constitutively expressed extracellular collagenolytic U32 peptidase in these bacteria is unclear. |
| Databáze: | OpenAIRE |
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