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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Online Access:http://citeseerx.ist.psu.edu/viewdoc/summary?doi=10.1.1.534.6730
http://www.genomed-dna.com/literatur/Star/18754.pdf
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spelling ftciteseerx:oai:CiteSeerX.psu:10.1.1.534.6730 2023-05-15T13:37:47+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* The Pennsylvania State University CiteSeerX Archives application/pdf http://citeseerx.ist.psu.edu/viewdoc/summary?doi=10.1.1.534.6730 http://www.genomed-dna.com/literatur/Star/18754.pdf en eng http://citeseerx.ist.psu.edu/viewdoc/summary?doi=10.1.1.534.6730 http://www.genomed-dna.com/literatur/Star/18754.pdf Metadata may be used without restrictions as long as the oai identifier remains attached to it. http://www.genomed-dna.com/literatur/Star/18754.pdf text ftciteseerx 2016-01-08T10:45:58Z 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 pre-dicted secondary structure displays a structural and functional organization in two modules similar to that of H-NS in Escherichia coli. Remarkably, the Acineto-bacter protein fully restores to the wild-type H-NS-de-pendent phenotypes, whereas the Psychrobacter protein is no longer able to reverse the effects of H-NS defi-ciency in an E. coli mutant strain above 30 °C. Moreover, in vitro experiments demonstrate that the ability of the Text Antarc* Antarctic Antarctica Siberia Unknown Antarctic
institution Open Polar
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op_collection_id ftciteseerx
language English
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 pre-dicted secondary structure displays a structural and functional organization in two modules similar to that of H-NS in Escherichia coli. Remarkably, the Acineto-bacter protein fully restores to the wild-type H-NS-de-pendent phenotypes, whereas the Psychrobacter protein is no longer able to reverse the effects of H-NS defi-ciency in an E. coli mutant strain above 30 °C. Moreover, in vitro experiments demonstrate that the ability of the
author2 The Pennsylvania State University CiteSeerX Archives
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title A Novel H-NS-like Protein from an Antarctic Psychrophilic Bacterium Reveals a Crucial Role for the N-terminal Domain in Thermal Stability*
spellingShingle 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*
url http://citeseerx.ist.psu.edu/viewdoc/summary?doi=10.1.1.534.6730
http://www.genomed-dna.com/literatur/Star/18754.pdf
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Siberia
genre_facet Antarc*
Antarctic
Antarctica
Siberia
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http://www.genomed-dna.com/literatur/Star/18754.pdf
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