Functional activity of E. coli RNase R in the Antarctic Pseudomonas syringae Lz4W
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...
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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 |
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ftpubmed:oai:pubmedcentral.nih.gov:10579198 2023-11-12T04:07:39+01:00 Functional activity of E. coli RNase R in the Antarctic Pseudomonas syringae Lz4W Hussain, Ashaq Ray, Malay Kumar 2023-10-16 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 en eng Springer Berlin Heidelberg http://www.ncbi.nlm.nih.gov/pmc/articles/PMC10579198/ http://www.ncbi.nlm.nih.gov/pubmed/37843651 http://dx.doi.org/10.1186/s43141-023-00553-2 © Academy of Scientific Research and Technology 2023 https://creativecommons.org/licenses/by/4.0/Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) . J Genet Eng Biotechnol Research Text 2023 ftpubmed https://doi.org/10.1186/s43141-023-00553-2 2023-10-22T00:50:51Z 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. Text Antarc* Antarctic PubMed Central (PMC) Antarctic The Antarctic Journal of Genetic Engineering and Biotechnology 21 1 |
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Research Hussain, Ashaq Ray, Malay Kumar Functional activity of E. coli RNase R in the Antarctic Pseudomonas syringae Lz4W |
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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. |
format |
Text |
author |
Hussain, Ashaq Ray, Malay Kumar |
author_facet |
Hussain, Ashaq Ray, Malay Kumar |
author_sort |
Hussain, Ashaq |
title |
Functional activity of E. coli RNase R in the Antarctic Pseudomonas syringae Lz4W |
title_short |
Functional activity of E. coli RNase R in the Antarctic Pseudomonas syringae Lz4W |
title_full |
Functional activity of E. coli RNase R in the Antarctic Pseudomonas syringae Lz4W |
title_fullStr |
Functional activity of E. coli RNase R in the Antarctic Pseudomonas syringae Lz4W |
title_full_unstemmed |
Functional activity of E. coli RNase R in the Antarctic Pseudomonas syringae Lz4W |
title_sort |
functional activity of e. coli rnase r in the antarctic pseudomonas syringae lz4w |
publisher |
Springer Berlin Heidelberg |
publishDate |
2023 |
url |
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 |
geographic |
Antarctic The Antarctic |
geographic_facet |
Antarctic The Antarctic |
genre |
Antarc* Antarctic |
genre_facet |
Antarc* Antarctic |
op_source |
J Genet Eng Biotechnol |
op_relation |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC10579198/ http://www.ncbi.nlm.nih.gov/pubmed/37843651 http://dx.doi.org/10.1186/s43141-023-00553-2 |
op_rights |
© Academy of Scientific Research and Technology 2023 https://creativecommons.org/licenses/by/4.0/Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) . |
op_doi |
https://doi.org/10.1186/s43141-023-00553-2 |
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Journal of Genetic Engineering and Biotechnology |
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21 |
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1 |
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