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

IF 3.6 Q2 BIOTECHNOLOGY & APPLIED MICROBIOLOGY Journal, genetic engineering & biotechnology Pub Date : 2023-10-16 DOI:10.1186/s43141-023-00553-2
Ashaq Hussain, Malay Kumar Ray
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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 expressing the RNBEc (catalytic domain of E. coli RNase R) displayed longer lag phase than the RNBPs (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 REc) rescues the cold-sensitive phenotype of the P. syringae Δrnr mutant. Similarly, the catalytic domain of E. coli RNase R (RNBEc) 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.

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南极丁香假单胞菌Lz4W中大肠杆菌RNase R的功能活性。
背景:在南极,丁香RNase R在16S和5S rRNA的加工中起着重要作用,从而在细菌的冷适应生长中发挥着重要作用。本研究的重点是在一种进化遥远的嗜冷细菌Pseudomonas syringae Lz4W中解读嗜中温外核糖核酸酶R及其催化结构域(RNB)的体内功能活性丁香假单胞菌∆rnr突变体。更重要的是,大肠杆菌核糖核酸酶R的催化结构域(RNB)也能够减轻∆rnr突变体的冷敏感生长缺陷,正如丁香花假单胞菌酶的催化结构区(RNB)所见。在4°C下,大肠杆菌RNase R的催化结构域在拯救∆rnr突变体的冷敏生长方面不如丁香花RNase R催化结构域有效,因为表达RNBEc(大肠杆菌RNaseR催化结构区)的∆rnr在4°C.时比RNBPs(丁香花RNaseR的催化域)补充的∆rnr突变体显示出更长的滞后期。总之,在低温(4°C)下,大肠杆菌RNase R和丁香花RNase R在功能上可交换丁香花的生长需求。我们的结果还证实,在丁香中,支持4°C生长的RNase R的需求与脱颗粒体复合体无关。结论:大肠杆菌RNase R(RNase REc)挽救了丁香花Δrnr突变体的冷敏表型。同样,大肠杆菌核糖核酸酶R(RNBEc)的催化结构域也能够在低温下支持Δrnr突变体的生长。这些发现在基于低温的表达系统的设计和开发中具有广阔的范围。
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