A Novel H-NS-like protein from an antarctic psychrophilic bacterium reveals a crucial role for the N-terminal domain in thermal stability
We describe here new members of the H-NS protein family identified in a psychrotrophic Acinetobacter spp. bacterium collected in Siberia and in a psychrophilic Psychrobacter spp. bacterium collected in Antarctica. Both are phylogenetically closely related to the HvrA and SPB Rhodobacter transcriptio...
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American Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.jbc.org/
2003
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Online Access: | https://doi.org/10.1074/jbc.M211766200 http://hdl.handle.net/10722/225141 |
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ftunivhongkonghu:oai:hub.hku.hk:10722/225141 2023-05-15T13:52:01+02:00 A Novel H-NS-like protein from an antarctic psychrophilic bacterium reveals a crucial role for the N-terminal domain in thermal stability Soutourina, OA Danchin, A Bertin, PN Tendeng, C Krin, E Marin, A 2003 https://doi.org/10.1074/jbc.M211766200 http://hdl.handle.net/10722/225141 eng eng American Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.jbc.org/ United States Journal of Biological Chemistry Journal of Biological Chemistry, 2003, v. 278 n. 21, p. 18754-18760 doi:10.1074/jbc.M211766200 18760 95510 0021-9258 21 12637536 18754 http://hdl.handle.net/10722/225141 278 Journal of Biological Chemistry. Copyright © American Society for Biochemistry and Molecular Biology, Inc. This research was originally published in [Journal Name]. Author(s). Title. Journal Name. Year. Vol:pp-pp. © the American Society for Biochemistry and Molecular Biology Acinetobacter - chemistry Bacterial Proteins - chemistry - metabolism DNA-Binding Proteins - chemistry - metabolism Gammaproteobacteria - chemistry Rhodobacter capsulatus - chemistry Article 2003 ftunivhongkonghu https://doi.org/10.1074/jbc.M211766200 2023-01-14T16:12:46Z We describe here new members of the H-NS protein family identified in a psychrotrophic Acinetobacter spp. bacterium collected in Siberia and in a psychrophilic Psychrobacter spp. bacterium collected in Antarctica. Both are phylogenetically closely related to the HvrA and SPB Rhodobacter transcriptional regulators. Their amino acid sequence shares 40% identity, and their predicted secondary structure displays a structural and functional organization in two modules similar to that of H-NS in Escherichia coli. Remarkably, the Acinetobacter protein fully restores to the wild-type H-NS-dependent phenotypes, whereas the Psychrobacter protein is no longer able to reverse the effects of H-NS deficiency in an E. coli mutant strain above 30 degrees C. Moreover, in vitro experiments demonstrate that the ability of the Psychrobacter H-NS protein to bind curved DNA and to form dimers is altered at 37 degrees C. The construction of hybrid proteins containing the N- or the C-terminal part of E. coli H-NS fused to the C- or N-terminal part of the Psychrobacter protein demonstrates the role of the N-terminal domain in this process. Finally, circular dichroism analysis of purified H-NS proteins suggests that, as compared with the E. coli and Acinetobacter proteins, the alpha-helical domain displays weaker intermolecular interactions in the Psychrobacter protein, which may account for the low thermal stability observed at 37 degrees C. Article in Journal/Newspaper Antarc* Antarctic Antarctica Siberia University of Hong Kong: HKU Scholars Hub Antarctic Journal of Biological Chemistry 278 21 18754 18760 |
institution |
Open Polar |
collection |
University of Hong Kong: HKU Scholars Hub |
op_collection_id |
ftunivhongkonghu |
language |
English |
topic |
Acinetobacter - chemistry Bacterial Proteins - chemistry - metabolism DNA-Binding Proteins - chemistry - metabolism Gammaproteobacteria - chemistry Rhodobacter capsulatus - chemistry |
spellingShingle |
Acinetobacter - chemistry Bacterial Proteins - chemistry - metabolism DNA-Binding Proteins - chemistry - metabolism Gammaproteobacteria - chemistry Rhodobacter capsulatus - chemistry Soutourina, OA Danchin, A Bertin, PN Tendeng, C Krin, E Marin, A A Novel H-NS-like protein from an antarctic psychrophilic bacterium reveals a crucial role for the N-terminal domain in thermal stability |
topic_facet |
Acinetobacter - chemistry Bacterial Proteins - chemistry - metabolism DNA-Binding Proteins - chemistry - metabolism Gammaproteobacteria - chemistry Rhodobacter capsulatus - chemistry |
description |
We describe here new members of the H-NS protein family identified in a psychrotrophic Acinetobacter spp. bacterium collected in Siberia and in a psychrophilic Psychrobacter spp. bacterium collected in Antarctica. Both are phylogenetically closely related to the HvrA and SPB Rhodobacter transcriptional regulators. Their amino acid sequence shares 40% identity, and their predicted secondary structure displays a structural and functional organization in two modules similar to that of H-NS in Escherichia coli. Remarkably, the Acinetobacter protein fully restores to the wild-type H-NS-dependent phenotypes, whereas the Psychrobacter protein is no longer able to reverse the effects of H-NS deficiency in an E. coli mutant strain above 30 degrees C. Moreover, in vitro experiments demonstrate that the ability of the Psychrobacter H-NS protein to bind curved DNA and to form dimers is altered at 37 degrees C. The construction of hybrid proteins containing the N- or the C-terminal part of E. coli H-NS fused to the C- or N-terminal part of the Psychrobacter protein demonstrates the role of the N-terminal domain in this process. Finally, circular dichroism analysis of purified H-NS proteins suggests that, as compared with the E. coli and Acinetobacter proteins, the alpha-helical domain displays weaker intermolecular interactions in the Psychrobacter protein, which may account for the low thermal stability observed at 37 degrees C. |
format |
Article in Journal/Newspaper |
author |
Soutourina, OA Danchin, A Bertin, PN Tendeng, C Krin, E Marin, A |
author_facet |
Soutourina, OA Danchin, A Bertin, PN Tendeng, C Krin, E Marin, A |
author_sort |
Soutourina, OA |
title |
A Novel H-NS-like protein from an antarctic psychrophilic bacterium reveals a crucial role for the N-terminal domain in thermal stability |
title_short |
A Novel H-NS-like protein from an antarctic psychrophilic bacterium reveals a crucial role for the N-terminal domain in thermal stability |
title_full |
A Novel H-NS-like protein from an antarctic psychrophilic bacterium reveals a crucial role for the N-terminal domain in thermal stability |
title_fullStr |
A Novel H-NS-like protein from an antarctic psychrophilic bacterium reveals a crucial role for the N-terminal domain in thermal stability |
title_full_unstemmed |
A Novel H-NS-like protein from an antarctic psychrophilic bacterium reveals a crucial role for the N-terminal domain in thermal stability |
title_sort |
novel h-ns-like protein from an antarctic psychrophilic bacterium reveals a crucial role for the n-terminal domain in thermal stability |
publisher |
American Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.jbc.org/ |
publishDate |
2003 |
url |
https://doi.org/10.1074/jbc.M211766200 http://hdl.handle.net/10722/225141 |
geographic |
Antarctic |
geographic_facet |
Antarctic |
genre |
Antarc* Antarctic Antarctica Siberia |
genre_facet |
Antarc* Antarctic Antarctica Siberia |
op_relation |
Journal of Biological Chemistry Journal of Biological Chemistry, 2003, v. 278 n. 21, p. 18754-18760 doi:10.1074/jbc.M211766200 18760 95510 0021-9258 21 12637536 18754 http://hdl.handle.net/10722/225141 278 |
op_rights |
Journal of Biological Chemistry. Copyright © American Society for Biochemistry and Molecular Biology, Inc. This research was originally published in [Journal Name]. Author(s). Title. Journal Name. Year. Vol:pp-pp. © the American Society for Biochemistry and Molecular Biology |
op_doi |
https://doi.org/10.1074/jbc.M211766200 |
container_title |
Journal of Biological Chemistry |
container_volume |
278 |
container_issue |
21 |
container_start_page |
18754 |
op_container_end_page |
18760 |
_version_ |
1766256169190424576 |