Functional activity of E. coli RNase R in the Antarctic Pseudomonas syringae Lz4W

• Published in: Journal of Genetic Engineering and Biotechnology
• Main Authors: Hussain, Ashaq, Ray, Malay Kumar
• Format: Text
• Language: English
• Published: Springer Berlin Heidelberg 2023
• Subjects: Research; Antarctic; The Antarctic; Antarc*
• Online Access: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC10579198/; http://www.ncbi.nlm.nih.gov/pubmed/37843651; https://doi.org/10.1186/s43141-023-00553-2

BACKGROUND: In Antarctic P. syringae RNase R play an essential role in the processing of 16S and 5S rRNA, thereby playing an important role in cold-adapted growth of the bacterium. This study is focused on deciphering the in vivo functional activity of mesophilic exoribonuclease R and its catalytic domain (RNB) in an evolutionary distant psychrophilic bacterium Pseudomonas syringae Lz4W. RESULTS: Our results confirm that E. coli RNase R complemented the physiological functions of the psychrophilic bacterium P. syringae RNase R and rescued the cold-sensitive phenotype of Pseudomonas syringae ∆rnr mutant. More importantly, the catalytic domain (RNB) of the E. coli RNase R is also capable of alleviating the cold-sensitive growth defects of ∆rnr mutant as seen with the catalytic domain (RNB) of the P. syringae enzyme. The Catalytic domain of E. coli RNase R was less efficient than the Catalytic domain of P. syringae RNase R in rescuing the cold-sensitive growth of ∆rnr mutant at 4°C, as the ∆rnr expressing the RNB(Ec) (catalytic domain of E. coli RNase R) displayed longer lag phase than the RNB(Ps) (Catalytic domain of P. syringae RNase R) complemented ∆rnr mutant at 4°C. Altogether it appears that the E. coli RNase R and P. syringae RNase R are functionally exchangeable for the growth requirements of P. syringae at low temperature (4°C). Our results also confirm that in P. syringae the requirement of RNase R for supporting the growth at 4°C is independent of the degradosomal complex. CONCLUSION: E. coli RNase R (RNase R(Ec)) rescues the cold-sensitive phenotype of the P. syringae Δrnr mutant. Similarly, the catalytic domain of E. coli RNase R (RNB(Ec)) is also capable of supporting the growth of Δrnr mutant at low temperatures. These findings have a vast scope in the design and development of low-temperature-based expression systems. SUPPLEMENTARY INFORMATION: The online version contains supplementary material available at 10.1186/s43141-023-00553-2.