A novel thermostable and halophilic thioredoxin reductase from the Red Sea Atlantis II hot brine pool

Autor: Mahmoud M. Said, Amr Y. Esmat, Ahmed A. Sayed, Elham A. Badiea, Walid M. Fouad, Mohamad Maged
Jazyk: angličtina
Rok vydání: 2019
Předmět:
Aquatic Organisms
Thioredoxin reductase
Biochemistry
Database and Informatics Methods
Enzyme Stability
Electrochemistry
Salt Bridges
Indian Ocean
Phylogeny
chemistry.chemical_classification
0303 health sciences
Multidisciplinary
Microbiota
Temperature
Halophile
Enzymes
Chemistry
Brine
Physical Sciences
Medicine
Thioredoxin
Water Microbiology
Sequence Analysis
Research Article
Multiple Alignment Calculation
Thioredoxin-Disulfide Reductase
Bioinformatics
Science
Brine pool
Research and Analysis Methods
03 medical and health sciences
Amino Acid Sequence Analysis
Protein Domains
Sequence Motif Analysis
Bodies of water
Computational Techniques
Seawater
Gene
030304 developmental biology
030306 microbiology
Thermophile
Biology and Life Sciences
Proteins
Red Sea
Split-Decomposition Method
Marine and aquatic sciences
Earth sciences
Enzyme
chemistry
Enzymology
Metagenome
Sequence Alignment
Zdroj: PLoS ONE, Vol 14, Iss 5, p e0217565 (2019)
PLoS ONE
ISSN: 1932-6203
Popis: The highly extreme conditions of the lower convective layer in the Atlantis II (ATII) Deep brine pool of the Red Sea make it an ideal environment for the search for novel enzymes that can function under extreme conditions. In the current study, we isolated a novel sequence of a thioredoxin reductase (TrxR) enzyme from the metagenomic dataset established from the microbial community that resides in the lower convective layer of Atlantis II. The gene was cloned, expressed and characterized for redox activity, halophilicity, and thermal stability. The isolated thioredoxin reductase (ATII-TrxR) was found to belong to the high-molecular-weight class of thioredoxin reductases. A search for conserved domains revealed the presence of an extra domain (Crp) in the enzyme sequence. Characterization studies of ATII-TrxR revealed that the enzyme was halophilic (maintained activity at 4 M NaCl), thermophilic (optimum temperature was 65°C) and thermostable (60% of its activity was retained at 70°C). Additionally, the enzyme utilized NADH in addition to NADPH as an electron donor. In conclusion, a novel thermostable and halophilic thioredoxin reductase has been isolated with a unique sequence that adapts to the harsh conditions of the brine pools making this protein a good candidate for biological research and industrial applications.
Databáze: OpenAIRE
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