CspB of an arctic bacterium, Polaribacter irgensii KOPRI 22228, confers extraordinary freeze-tolerance
Freezing temperatures are a major challenge for life at the poles. Decreased membrane fluidity, uninvited secondary structure formation in nucleic acids, and protein cold-denaturation all occur at cold temperatures. Organisms adapted to polar regions possess distinct mechanisms that enable them to s...
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ftpubmed:oai:pubmedcentral.nih.gov:5790591 2023-05-15T14:57:42+02:00 CspB of an arctic bacterium, Polaribacter irgensii KOPRI 22228, confers extraordinary freeze-tolerance Jung, Youn Hong Lee, Yoo Kyung Lee, Hong Kum Lee, Kyunghee Im, Hana 2017-07-31 http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5790591/ http://www.ncbi.nlm.nih.gov/pubmed/28807609 https://doi.org/10.1016/j.bjm.2017.04.006 en eng Elsevier http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5790591/ http://www.ncbi.nlm.nih.gov/pubmed/28807609 http://dx.doi.org/10.1016/j.bjm.2017.04.006 © 2017 Sociedade Brasileira de Microbiologia. Published by Elsevier Editora Ltda. http://creativecommons.org/licenses/by-nc-nd/4.0/ This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/). CC-BY-NC-ND Research Paper Text 2017 ftpubmed https://doi.org/10.1016/j.bjm.2017.04.006 2018-02-04T01:34:12Z Freezing temperatures are a major challenge for life at the poles. Decreased membrane fluidity, uninvited secondary structure formation in nucleic acids, and protein cold-denaturation all occur at cold temperatures. Organisms adapted to polar regions possess distinct mechanisms that enable them to survive in extremely cold environments. Among the cold-induced proteins, cold shock protein (Csp) family proteins are the most prominent. A gene coding for a Csp-family protein, cspB, was cloned from an arctic bacterium, Polaribacter irgensii KOPRI 22228, and overexpression of cspB greatly increased the freeze-survival rates of Escherichia coli hosts, to a greater level than any previously reported Csp. It also suppressed the cold-sensitivity of an E. coli csp-quadruple deletion strain, BX04. Sequence analysis showed that this protein consists of a unique domain at its N-terminal end and a well conserved cold shock domain at its C-terminal end. The most common mechanism of Csp function in cold adaption is melting of the secondary structures in RNA and DNA molecules, thus facilitating transcription and translation at low temperatures. P. irgensii CspB bound to oligo(dT)-cellulose resins, suggesting single-stranded nucleic acid-binding activity. The unprecedented level of freeze-tolerance conferred by P. irgensii CspB suggests a crucial role for this protein in survival in polar environments. Text Arctic PubMed Central (PMC) Arctic Brazilian Journal of Microbiology 49 1 97 103 |
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Research Paper Jung, Youn Hong Lee, Yoo Kyung Lee, Hong Kum Lee, Kyunghee Im, Hana CspB of an arctic bacterium, Polaribacter irgensii KOPRI 22228, confers extraordinary freeze-tolerance |
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Research Paper |
description |
Freezing temperatures are a major challenge for life at the poles. Decreased membrane fluidity, uninvited secondary structure formation in nucleic acids, and protein cold-denaturation all occur at cold temperatures. Organisms adapted to polar regions possess distinct mechanisms that enable them to survive in extremely cold environments. Among the cold-induced proteins, cold shock protein (Csp) family proteins are the most prominent. A gene coding for a Csp-family protein, cspB, was cloned from an arctic bacterium, Polaribacter irgensii KOPRI 22228, and overexpression of cspB greatly increased the freeze-survival rates of Escherichia coli hosts, to a greater level than any previously reported Csp. It also suppressed the cold-sensitivity of an E. coli csp-quadruple deletion strain, BX04. Sequence analysis showed that this protein consists of a unique domain at its N-terminal end and a well conserved cold shock domain at its C-terminal end. The most common mechanism of Csp function in cold adaption is melting of the secondary structures in RNA and DNA molecules, thus facilitating transcription and translation at low temperatures. P. irgensii CspB bound to oligo(dT)-cellulose resins, suggesting single-stranded nucleic acid-binding activity. The unprecedented level of freeze-tolerance conferred by P. irgensii CspB suggests a crucial role for this protein in survival in polar environments. |
format |
Text |
author |
Jung, Youn Hong Lee, Yoo Kyung Lee, Hong Kum Lee, Kyunghee Im, Hana |
author_facet |
Jung, Youn Hong Lee, Yoo Kyung Lee, Hong Kum Lee, Kyunghee Im, Hana |
author_sort |
Jung, Youn Hong |
title |
CspB of an arctic bacterium, Polaribacter irgensii KOPRI 22228, confers extraordinary freeze-tolerance |
title_short |
CspB of an arctic bacterium, Polaribacter irgensii KOPRI 22228, confers extraordinary freeze-tolerance |
title_full |
CspB of an arctic bacterium, Polaribacter irgensii KOPRI 22228, confers extraordinary freeze-tolerance |
title_fullStr |
CspB of an arctic bacterium, Polaribacter irgensii KOPRI 22228, confers extraordinary freeze-tolerance |
title_full_unstemmed |
CspB of an arctic bacterium, Polaribacter irgensii KOPRI 22228, confers extraordinary freeze-tolerance |
title_sort |
cspb of an arctic bacterium, polaribacter irgensii kopri 22228, confers extraordinary freeze-tolerance |
publisher |
Elsevier |
publishDate |
2017 |
url |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5790591/ http://www.ncbi.nlm.nih.gov/pubmed/28807609 https://doi.org/10.1016/j.bjm.2017.04.006 |
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Arctic |
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Arctic |
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Arctic |
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Arctic |
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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5790591/ http://www.ncbi.nlm.nih.gov/pubmed/28807609 http://dx.doi.org/10.1016/j.bjm.2017.04.006 |
op_rights |
© 2017 Sociedade Brasileira de Microbiologia. Published by Elsevier Editora Ltda. http://creativecommons.org/licenses/by-nc-nd/4.0/ This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/). |
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CC-BY-NC-ND |
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https://doi.org/10.1016/j.bjm.2017.04.006 |
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Brazilian Journal of Microbiology |
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49 |
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1 |
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97 |
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103 |
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1766329822638768128 |