A Novel Cold-Adapted and Salt-Tolerant RNase R from Antarctic Sea-Ice Bacterium Psychrobacter sp. ANT206
A novel RNase R, psrnr, was cloned from the Antarctic bacterium Psychrobacter sp. ANT206 and expressed in Escherichia coli (E. coli). A bioinformatics analysis of the psrnr gene revealed that it contained an open reading frame of 2313 bp and encoded a protein (PsRNR) of 770 amino acids. Homology mod...
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ftpubmed:oai:pubmedcentral.nih.gov:6630635 2023-05-15T13:57:24+02:00 A Novel Cold-Adapted and Salt-Tolerant RNase R from Antarctic Sea-Ice Bacterium Psychrobacter sp. ANT206 Wang, Yatong Hou, Yanhua Nie, Ping Wang, Yifan Ren, Xiulian Wei, Qifeng Wang, Quanfu 2019-06-14 http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6630635/ http://www.ncbi.nlm.nih.gov/pubmed/31207974 https://doi.org/10.3390/molecules24122229 en eng MDPI http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6630635/ http://www.ncbi.nlm.nih.gov/pubmed/31207974 http://dx.doi.org/10.3390/molecules24122229 © 2019 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/). CC-BY Article Text 2019 ftpubmed https://doi.org/10.3390/molecules24122229 2019-08-25T00:11:25Z A novel RNase R, psrnr, was cloned from the Antarctic bacterium Psychrobacter sp. ANT206 and expressed in Escherichia coli (E. coli). A bioinformatics analysis of the psrnr gene revealed that it contained an open reading frame of 2313 bp and encoded a protein (PsRNR) of 770 amino acids. Homology modeling indicated that PsRNR had reduced hydrogen bonds and salt bridges, which might be the main reason for the catalytic efficiency at low temperatures. A site directed mutation exhibited that His 667 in the active site was absolutely crucial for the enzyme catalysis. The recombinant PsRNR (rPsRNR) showed maximum activity at 30 °C and had thermal instability, suggesting that rPsRNR was a cold-adapted enzyme. Interestingly, rPsRNR displayed remarkable salt tolerance, remaining stable at 0.5–3.0 M NaCl. Furthermore, rPsRNR had a higher k(cat) value, contributing to its efficient catalytic activity at a low temperature. Overall, cold-adapted RNase R in this study was an excellent candidate for antimicrobial treatment. Text Antarc* Antarctic Sea ice PubMed Central (PMC) Antarctic The Antarctic Molecules 24 12 2229 |
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Article Wang, Yatong Hou, Yanhua Nie, Ping Wang, Yifan Ren, Xiulian Wei, Qifeng Wang, Quanfu A Novel Cold-Adapted and Salt-Tolerant RNase R from Antarctic Sea-Ice Bacterium Psychrobacter sp. ANT206 |
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description |
A novel RNase R, psrnr, was cloned from the Antarctic bacterium Psychrobacter sp. ANT206 and expressed in Escherichia coli (E. coli). A bioinformatics analysis of the psrnr gene revealed that it contained an open reading frame of 2313 bp and encoded a protein (PsRNR) of 770 amino acids. Homology modeling indicated that PsRNR had reduced hydrogen bonds and salt bridges, which might be the main reason for the catalytic efficiency at low temperatures. A site directed mutation exhibited that His 667 in the active site was absolutely crucial for the enzyme catalysis. The recombinant PsRNR (rPsRNR) showed maximum activity at 30 °C and had thermal instability, suggesting that rPsRNR was a cold-adapted enzyme. Interestingly, rPsRNR displayed remarkable salt tolerance, remaining stable at 0.5–3.0 M NaCl. Furthermore, rPsRNR had a higher k(cat) value, contributing to its efficient catalytic activity at a low temperature. Overall, cold-adapted RNase R in this study was an excellent candidate for antimicrobial treatment. |
format |
Text |
author |
Wang, Yatong Hou, Yanhua Nie, Ping Wang, Yifan Ren, Xiulian Wei, Qifeng Wang, Quanfu |
author_facet |
Wang, Yatong Hou, Yanhua Nie, Ping Wang, Yifan Ren, Xiulian Wei, Qifeng Wang, Quanfu |
author_sort |
Wang, Yatong |
title |
A Novel Cold-Adapted and Salt-Tolerant RNase R from Antarctic Sea-Ice Bacterium Psychrobacter sp. ANT206 |
title_short |
A Novel Cold-Adapted and Salt-Tolerant RNase R from Antarctic Sea-Ice Bacterium Psychrobacter sp. ANT206 |
title_full |
A Novel Cold-Adapted and Salt-Tolerant RNase R from Antarctic Sea-Ice Bacterium Psychrobacter sp. ANT206 |
title_fullStr |
A Novel Cold-Adapted and Salt-Tolerant RNase R from Antarctic Sea-Ice Bacterium Psychrobacter sp. ANT206 |
title_full_unstemmed |
A Novel Cold-Adapted and Salt-Tolerant RNase R from Antarctic Sea-Ice Bacterium Psychrobacter sp. ANT206 |
title_sort |
novel cold-adapted and salt-tolerant rnase r from antarctic sea-ice bacterium psychrobacter sp. ant206 |
publisher |
MDPI |
publishDate |
2019 |
url |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6630635/ http://www.ncbi.nlm.nih.gov/pubmed/31207974 https://doi.org/10.3390/molecules24122229 |
geographic |
Antarctic The Antarctic |
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Antarctic The Antarctic |
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Antarc* Antarctic Sea ice |
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Antarc* Antarctic Sea ice |
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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6630635/ http://www.ncbi.nlm.nih.gov/pubmed/31207974 http://dx.doi.org/10.3390/molecules24122229 |
op_rights |
© 2019 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/). |
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CC-BY |
op_doi |
https://doi.org/10.3390/molecules24122229 |
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Molecules |
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