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A Novel Cold-Adapted and Salt-Tolerant RNase R from Antarctic Sea-Ice Bacterium Psychrobacter sp. ANT206.
- Source :
-
Molecules (Basel, Switzerland) [Molecules] 2019 Jun 14; Vol. 24 (12). Date of Electronic Publication: 2019 Jun 14. - Publication Year :
- 2019
-
Abstract
- A novel RNase R, psrnr , was cloned from the Antarctic bacterium Psychrobacter sp. ANT206 and expressed in Escherichia coli ( E. coli ). A bioinformatics analysis of the psrnr gene revealed that it contained an open reading frame of 2313 bp and encoded a protein (PsRNR) of 770 amino acids. Homology modeling indicated that PsRNR had reduced hydrogen bonds and salt bridges, which might be the main reason for the catalytic efficiency at low temperatures. A site directed mutation exhibited that His 667 in the active site was absolutely crucial for the enzyme catalysis. The recombinant PsRNR (rPsRNR) showed maximum activity at 30 °C and had thermal instability, suggesting that rPsRNR was a cold-adapted enzyme. Interestingly, rPsRNR displayed remarkable salt tolerance, remaining stable at 0.5-3.0 M NaCl. Furthermore, rPsRNR had a higher k <subscript>cat</subscript> value, contributing to its efficient catalytic activity at a low temperature. Overall, cold-adapted RNase R in this study was an excellent candidate for antimicrobial treatment.
- Subjects :
- Amino Acid Sequence
Antarctic Regions
Bacterial Proteins chemistry
Bacterial Proteins genetics
Enzyme Activation
Kinetics
Models, Biological
Molecular Conformation
Molecular Structure
Psychrobacter isolation & purification
Ribonucleases genetics
Adaptation, Biological
Cold Temperature
Environmental Microbiology
Ice Cover microbiology
Psychrobacter physiology
Ribonucleases metabolism
Salt Tolerance
Subjects
Details
- Language :
- English
- ISSN :
- 1420-3049
- Volume :
- 24
- Issue :
- 12
- Database :
- MEDLINE
- Journal :
- Molecules (Basel, Switzerland)
- Publication Type :
- Academic Journal
- Accession number :
- 31207974
- Full Text :
- https://doi.org/10.3390/molecules24122229