The small heat shock proteins from <it>Acidithiobacillus ferrooxidans: </it>gene expression, phylogenetic analysis, and structural modeling

<p>Abstract</p> <p>Background</p> <p><it>Acidithiobacillus ferrooxidans </it>is an acidophilic, chemolithoautotrophic bacterium that has been successfully used in metal bioleaching. In this study, an analysis of the <it>A. ferrooxidans </it>ATCC...

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Main Authors: Ribeiro Daniela A, Del Bem Luiz EV, Vicentini Renato, Ferraz Lúcio FC, Murakami Mario T, Ottoboni Laura MM
Format: Article
Language:English
Published: BMC 2011-12-01
Series:BMC Microbiology
Online Access:http://www.biomedcentral.com/1471-2180/11/259
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spelling doaj-1d16b1ed3ec448f08e4719df70c2ccfd2020-11-25T00:15:11ZengBMCBMC Microbiology1471-21802011-12-0111125910.1186/1471-2180-11-259The small heat shock proteins from <it>Acidithiobacillus ferrooxidans: </it>gene expression, phylogenetic analysis, and structural modelingRibeiro Daniela ADel Bem Luiz EVVicentini RenatoFerraz Lúcio FCMurakami Mario TOttoboni Laura MM<p>Abstract</p> <p>Background</p> <p><it>Acidithiobacillus ferrooxidans </it>is an acidophilic, chemolithoautotrophic bacterium that has been successfully used in metal bioleaching. In this study, an analysis of the <it>A. ferrooxidans </it>ATCC 23270 genome revealed the presence of three sHSP genes, Afe_1009, Afe_1437 and Afe_2172, that encode proteins from the HSP20 family, a class of intracellular multimers that is especially important in extremophile microorganisms.</p> <p>Results</p> <p>The expression of the sHSP genes was investigated in <it>A. ferrooxidans </it>cells submitted to a heat shock at 40°C for 15, 30 and 60 minutes. After 60 minutes, the gene on locus Afe_1437 was about 20-fold more highly expressed than the gene on locus Afe_2172. Bioinformatic and phylogenetic analyses showed that the sHSPs from <it>A. ferrooxidans </it>are possible non-paralogous proteins, and are regulated by the σ<sup>32 </sup>factor, a common transcription factor of heat shock proteins. Structural studies using homology molecular modeling indicated that the proteins encoded by Afe_1009 and Afe_1437 have a conserved α-crystallin domain and share similar structural features with the sHSP from <it>Methanococcus jannaschii</it>, suggesting that their biological assembly involves 24 molecules and resembles a hollow spherical shell.</p> <p>Conclusion</p> <p>We conclude that the sHSPs encoded by the Afe_1437 and Afe_1009 genes are more likely to act as molecular chaperones in the <it>A. ferrooxidans </it>heat shock response. In addition, the three sHSPs from <it>A. ferrooxidans </it>are not recent paralogs, and the Afe_1437 and Afe_1009 genes could be inherited horizontally by <it>A. ferrooxidans</it>.</p> http://www.biomedcentral.com/1471-2180/11/259
collection DOAJ
language English
format Article
sources DOAJ
author Ribeiro Daniela A
Del Bem Luiz EV
Vicentini Renato
Ferraz Lúcio FC
Murakami Mario T
Ottoboni Laura MM
spellingShingle Ribeiro Daniela A
Del Bem Luiz EV
Vicentini Renato
Ferraz Lúcio FC
Murakami Mario T
Ottoboni Laura MM
The small heat shock proteins from <it>Acidithiobacillus ferrooxidans: </it>gene expression, phylogenetic analysis, and structural modeling
BMC Microbiology
author_facet Ribeiro Daniela A
Del Bem Luiz EV
Vicentini Renato
Ferraz Lúcio FC
Murakami Mario T
Ottoboni Laura MM
author_sort Ribeiro Daniela A
title The small heat shock proteins from <it>Acidithiobacillus ferrooxidans: </it>gene expression, phylogenetic analysis, and structural modeling
title_short The small heat shock proteins from <it>Acidithiobacillus ferrooxidans: </it>gene expression, phylogenetic analysis, and structural modeling
title_full The small heat shock proteins from <it>Acidithiobacillus ferrooxidans: </it>gene expression, phylogenetic analysis, and structural modeling
title_fullStr The small heat shock proteins from <it>Acidithiobacillus ferrooxidans: </it>gene expression, phylogenetic analysis, and structural modeling
title_full_unstemmed The small heat shock proteins from <it>Acidithiobacillus ferrooxidans: </it>gene expression, phylogenetic analysis, and structural modeling
title_sort small heat shock proteins from <it>acidithiobacillus ferrooxidans: </it>gene expression, phylogenetic analysis, and structural modeling
publisher BMC
series BMC Microbiology
issn 1471-2180
publishDate 2011-12-01
description <p>Abstract</p> <p>Background</p> <p><it>Acidithiobacillus ferrooxidans </it>is an acidophilic, chemolithoautotrophic bacterium that has been successfully used in metal bioleaching. In this study, an analysis of the <it>A. ferrooxidans </it>ATCC 23270 genome revealed the presence of three sHSP genes, Afe_1009, Afe_1437 and Afe_2172, that encode proteins from the HSP20 family, a class of intracellular multimers that is especially important in extremophile microorganisms.</p> <p>Results</p> <p>The expression of the sHSP genes was investigated in <it>A. ferrooxidans </it>cells submitted to a heat shock at 40°C for 15, 30 and 60 minutes. After 60 minutes, the gene on locus Afe_1437 was about 20-fold more highly expressed than the gene on locus Afe_2172. Bioinformatic and phylogenetic analyses showed that the sHSPs from <it>A. ferrooxidans </it>are possible non-paralogous proteins, and are regulated by the σ<sup>32 </sup>factor, a common transcription factor of heat shock proteins. Structural studies using homology molecular modeling indicated that the proteins encoded by Afe_1009 and Afe_1437 have a conserved α-crystallin domain and share similar structural features with the sHSP from <it>Methanococcus jannaschii</it>, suggesting that their biological assembly involves 24 molecules and resembles a hollow spherical shell.</p> <p>Conclusion</p> <p>We conclude that the sHSPs encoded by the Afe_1437 and Afe_1009 genes are more likely to act as molecular chaperones in the <it>A. ferrooxidans </it>heat shock response. In addition, the three sHSPs from <it>A. ferrooxidans </it>are not recent paralogs, and the Afe_1437 and Afe_1009 genes could be inherited horizontally by <it>A. ferrooxidans</it>.</p>
url http://www.biomedcentral.com/1471-2180/11/259
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