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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 kcat 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.
Highlights
Ribonuclease (Ribonuclease, RNase), an important nucleic acid hydrolase in organism, can hydrolyze the phosphodiester bonds among the nucleic acid residues of RNA and play a significant role in different stages of the cell metabolism [1,2]
In Escherichia coli (E. coli), eight distinct RNases involved in different aspects of RNA metabolism were identified
It has been discovered that RNase R in Pseudomonas syringae plays an important role in growth at low temperature [13]
Summary
Ribonuclease (Ribonuclease, RNase), an important nucleic acid hydrolase in organism, can hydrolyze the phosphodiester bonds among the nucleic acid residues of RNA and play a significant role in different stages of the cell metabolism [1,2]. A growing number of evidence has indicated that RNase R is a cold shock protein (CspA), and its expression regulation is closely related to microbial adaptation [10,11]. It is well-known that the recruitment of RNase R to the degradosome complex is related to its need for low temperatures during growth [12]. Due to the function of RNase R in RNA metabolism and biological activities [3,12], it might play an important role in the understanding of virulence associated with enterobacteria and have great value in antimicrobial treatment
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