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

• Main Authors: Hussain, Ashaq, Ray, Malay Kumar
• Format: Article in Journal/Newspaper
• Language: unknown
• Published: figshare 2023
• Subjects: Biophysics; Medicine; Microbiology; FOS Biological sciences; Cell Biology; Genetics; Immunology; FOS Clinical medicine; Developmental Biology; Infectious Diseases; FOS Health sciences; Virology; Computational Biology; Antarc*; Antarctic
• Online Access: https://dx.doi.org/10.6084/m9.figshare.c.6883495.v1; https://springernature.figshare.com/collections/Functional_activity_of_E_coli_RNase_R_in_the_Antarctic_Pseudomonas_syringae_Lz4W/6883495/1

Abstract 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 ...