Functional activity of E. coli RNase R in the Antarctic Pseudomonas syringae Lz4W ...
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 ca...
Main Authors: | , |
---|---|
Format: | Article in Journal/Newspaper |
Language: | unknown |
Published: |
figshare
2023
|
Subjects: | |
Online Access: | https://dx.doi.org/10.6084/m9.figshare.c.6883495 https://springernature.figshare.com/collections/Functional_activity_of_E_coli_RNase_R_in_the_Antarctic_Pseudomonas_syringae_Lz4W/6883495 |
id |
ftdatacite:10.6084/m9.figshare.c.6883495 |
---|---|
record_format |
openpolar |
spelling |
ftdatacite:10.6084/m9.figshare.c.6883495 2023-12-31T10:00:00+01:00 Functional activity of E. coli RNase R in the Antarctic Pseudomonas syringae Lz4W ... Hussain, Ashaq Ray, Malay Kumar 2023 https://dx.doi.org/10.6084/m9.figshare.c.6883495 https://springernature.figshare.com/collections/Functional_activity_of_E_coli_RNase_R_in_the_Antarctic_Pseudomonas_syringae_Lz4W/6883495 unknown figshare Creative Commons Attribution 4.0 International https://creativecommons.org/licenses/by/4.0/legalcode cc-by-4.0 Biophysics Medicine Microbiology FOS Biological sciences Cell Biology Genetics Immunology FOS Clinical medicine Developmental Biology Infectious Diseases FOS Health sciences Virology Computational Biology article Collection 2023 ftdatacite https://doi.org/10.6084/m9.figshare.c.6883495 2023-12-01T11:20:01Z 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 ... Article in Journal/Newspaper Antarc* Antarctic DataCite Metadata Store (German National Library of Science and Technology) |
institution |
Open Polar |
collection |
DataCite Metadata Store (German National Library of Science and Technology) |
op_collection_id |
ftdatacite |
language |
unknown |
topic |
Biophysics Medicine Microbiology FOS Biological sciences Cell Biology Genetics Immunology FOS Clinical medicine Developmental Biology Infectious Diseases FOS Health sciences Virology Computational Biology |
spellingShingle |
Biophysics Medicine Microbiology FOS Biological sciences Cell Biology Genetics Immunology FOS Clinical medicine Developmental Biology Infectious Diseases FOS Health sciences Virology Computational Biology Hussain, Ashaq Ray, Malay Kumar Functional activity of E. coli RNase R in the Antarctic Pseudomonas syringae Lz4W ... |
topic_facet |
Biophysics Medicine Microbiology FOS Biological sciences Cell Biology Genetics Immunology FOS Clinical medicine Developmental Biology Infectious Diseases FOS Health sciences Virology Computational Biology |
description |
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 ... |
format |
Article in Journal/Newspaper |
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 |
figshare |
publishDate |
2023 |
url |
https://dx.doi.org/10.6084/m9.figshare.c.6883495 https://springernature.figshare.com/collections/Functional_activity_of_E_coli_RNase_R_in_the_Antarctic_Pseudomonas_syringae_Lz4W/6883495 |
genre |
Antarc* Antarctic |
genre_facet |
Antarc* Antarctic |
op_rights |
Creative Commons Attribution 4.0 International https://creativecommons.org/licenses/by/4.0/legalcode cc-by-4.0 |
op_doi |
https://doi.org/10.6084/m9.figshare.c.6883495 |
_version_ |
1786844859861041152 |