CspB of an arctic bacterium, Polaribacter irgensii KOPRI 22228, confers extraordinary freeze-tolerance
ABSTRACT 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...
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ftjscielo:oai:scielo:S1517-83822018000100097 2023-05-15T14:58:42+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 2018-03-01 text/html http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822018000100097 en eng Sociedade Brasileira de Microbiologia 10.1016/j.bjm.2017.04.006 info:eu-repo/semantics/openAccess Brazilian Journal of Microbiology v.49 n.1 2018 Cold-shock protein (Csp) Psychrophile Cold-resistance info:eu-repo/semantics/article 2018 ftjscielo 2018-03-03T07:56:58Z ABSTRACT 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. Article in Journal/Newspaper Arctic SciELO Brazil (Scientific Electronic Library Online) Arctic |
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Open Polar |
collection |
SciELO Brazil (Scientific Electronic Library Online) |
op_collection_id |
ftjscielo |
language |
English |
topic |
Cold-shock protein (Csp) Psychrophile Cold-resistance |
spellingShingle |
Cold-shock protein (Csp) Psychrophile Cold-resistance 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 |
topic_facet |
Cold-shock protein (Csp) Psychrophile Cold-resistance |
description |
ABSTRACT 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 |
Article in Journal/Newspaper |
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 |
Sociedade Brasileira de Microbiologia |
publishDate |
2018 |
url |
http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822018000100097 |
geographic |
Arctic |
geographic_facet |
Arctic |
genre |
Arctic |
genre_facet |
Arctic |
op_source |
Brazilian Journal of Microbiology v.49 n.1 2018 |
op_relation |
10.1016/j.bjm.2017.04.006 |
op_rights |
info:eu-repo/semantics/openAccess |
_version_ |
1766330823927136256 |