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...
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ftdoajarticles:oai:doaj.org/article:c1c6732c9ef340a79e1ba99774180e34 2023-05-15T14:02:01+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 2019-06-01T00:00:00Z https://doi.org/10.3390/molecules24122229 https://doaj.org/article/c1c6732c9ef340a79e1ba99774180e34 EN eng MDPI AG https://www.mdpi.com/1420-3049/24/12/2229 https://doaj.org/toc/1420-3049 1420-3049 doi:10.3390/molecules24122229 https://doaj.org/article/c1c6732c9ef340a79e1ba99774180e34 Molecules, Vol 24, Iss 12, p 2229 (2019) RNase R cold-adapted antarctic bacterium sea-ice homology modeling Organic chemistry QD241-441 article 2019 ftdoajarticles https://doi.org/10.3390/molecules24122229 2022-12-31T08:16:57Z 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. Article in Journal/Newspaper Antarc* Antarctic Sea ice Directory of Open Access Journals: DOAJ Articles Antarctic The Antarctic Molecules 24 12 2229 |
institution |
Open Polar |
collection |
Directory of Open Access Journals: DOAJ Articles |
op_collection_id |
ftdoajarticles |
language |
English |
topic |
RNase R cold-adapted antarctic bacterium sea-ice homology modeling Organic chemistry QD241-441 |
spellingShingle |
RNase R cold-adapted antarctic bacterium sea-ice homology modeling Organic chemistry QD241-441 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 Organic chemistry QD241-441 |
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 |
Article in Journal/Newspaper |
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 |
MDPI AG |
publishDate |
2019 |
url |
https://doi.org/10.3390/molecules24122229 https://doaj.org/article/c1c6732c9ef340a79e1ba99774180e34 |
geographic |
Antarctic The Antarctic |
geographic_facet |
Antarctic The Antarctic |
genre |
Antarc* Antarctic Sea ice |
genre_facet |
Antarc* Antarctic Sea ice |
op_source |
Molecules, Vol 24, Iss 12, p 2229 (2019) |
op_relation |
https://www.mdpi.com/1420-3049/24/12/2229 https://doaj.org/toc/1420-3049 1420-3049 doi:10.3390/molecules24122229 https://doaj.org/article/c1c6732c9ef340a79e1ba99774180e34 |
op_doi |
https://doi.org/10.3390/molecules24122229 |
container_title |
Molecules |
container_volume |
24 |
container_issue |
12 |
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2229 |
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1766272090774700032 |