Back to Search Start Over

A Novel Cold-Adapted and Salt-Tolerant RNase R from Antarctic Sea-Ice Bacterium Psychrobacter sp. ANT206.

Authors :
Wang Y
Hou Y
Nie P
Wang Y
Ren X
Wei Q
Wang Q
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.

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