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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ftmdpi:oai:mdpi.com:/1420-3049/24/12/2229/ 2023-08-20T03:59:57+02:00 A Novel Cold-Adapted and Salt-Tolerant RNase R from Antarctic Sea-Ice Bacterium Psychrobacter sp. ANT206 Yatong Wang Yanhua Hou Ping Nie Yifan Wang Xiulian Ren Qifeng Wei Quanfu Wang agris 2019-06-14 application/pdf https://doi.org/10.3390/molecules24122229 EN eng Multidisciplinary Digital Publishing Institute Chemical Biology https://dx.doi.org/10.3390/molecules24122229 https://creativecommons.org/licenses/by/4.0/ Molecules; Volume 24; Issue 12; Pages: 2229 RNase R cold-adapted antarctic bacterium sea-ice homology modeling Text 2019 ftmdpi https://doi.org/10.3390/molecules24122229 2023-07-31T22:21:33Z 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 kcat 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 MDPI Open Access Publishing Antarctic The Antarctic Molecules 24 12 2229 |
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Open Polar |
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MDPI Open Access Publishing |
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ftmdpi |
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English |
topic |
RNase R cold-adapted antarctic bacterium sea-ice homology modeling |
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RNase R cold-adapted antarctic bacterium sea-ice homology modeling Yatong Wang Yanhua Hou Ping Nie Yifan Wang Xiulian Ren Qifeng Wei Quanfu Wang A Novel Cold-Adapted and Salt-Tolerant RNase R from Antarctic Sea-Ice Bacterium Psychrobacter sp. ANT206 |
topic_facet |
RNase R cold-adapted antarctic bacterium sea-ice homology modeling |
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 kcat 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 |
Yatong Wang Yanhua Hou Ping Nie Yifan Wang Xiulian Ren Qifeng Wei Quanfu Wang |
author_facet |
Yatong Wang Yanhua Hou Ping Nie Yifan Wang Xiulian Ren Qifeng Wei Quanfu Wang |
author_sort |
Yatong Wang |
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 |
Multidisciplinary Digital Publishing Institute |
publishDate |
2019 |
url |
https://doi.org/10.3390/molecules24122229 |
op_coverage |
agris |
geographic |
Antarctic The Antarctic |
geographic_facet |
Antarctic The Antarctic |
genre |
Antarc* Antarctic Sea ice |
genre_facet |
Antarc* Antarctic Sea ice |
op_source |
Molecules; Volume 24; Issue 12; Pages: 2229 |
op_relation |
Chemical Biology https://dx.doi.org/10.3390/molecules24122229 |
op_rights |
https://creativecommons.org/licenses/by/4.0/ |
op_doi |
https://doi.org/10.3390/molecules24122229 |
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Molecules |
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24 |
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12 |
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2229 |
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1774716188263186432 |