Novel Cell Envelope Proteins Related to Copper Resistance in Acidithiobacillus ferrooxidans

Rodrigo Almarcegui; Claudio Navarro; Alberto Paradela; Diego von Bernath; Carlos A. Jerez

doi:10.4028/www.scientific.net/AMR.825.206

Paper Titles

Analysis of the Bacterial Sulphur System
p.190

Heterodisulfide Reductase from Acidithiobacilli is a Key Component Involved in Metabolism of Reduced Inorganic Sulfur Compounds
p.194

Biogenesis and Transfer of Iron-Sulfur Clusters from Acidithiobacillus ferrooxidans
p.198

Evidence for Widespread Dissimilatory Hydrogen Metabolism among Acidophilic Bacteria
p.202

Novel Cell Envelope Proteins Related to Copper Resistance in Acidithiobacillus ferrooxidans
p.206

Conductive Filaments Produced by Aeromonas hydrophila
p.210

Comparative Study of Fluoride-Tolerance of Five Typical Bioleaching Microorganisms
p.214

Estimation of Ionic Load Effect on the Oxidizing Activity of the Microbial Population in the Heap Bioleaching Process at Escondida Mine
p.219

Biomediated Separation of Kaolinite and Hematite Using Bacillus subtilis
p.223

HomeAdvanced Materials ResearchAdvanced Materials Research Vol. 825Novel Cell Envelope Proteins Related to Copper...

Novel Cell Envelope Proteins Related to Copper Resistance in Acidithiobacillus ferrooxidans

Abstract:

The presence in At. ferrooxidans of canonical copper resistance determinants does not explain the extremely high copper concentrations this microorganism is able to tolerate. This suggests that At. ferrooxidans may have additional copper resistance mechanisms. New possible copper resistance determinants were searched by using 2D-PAGE and real time PCR (qRT-PCR). Results showed the up-regulation of RND-type Cus systems and different RND-type efflux pumps in At. ferrooxidans grown in the presence of copper, suggesting that these proteins may be implied in resistance to this metal. Furthermore, the up-regulation of putative periplasmatic disulfide isomerases was also seen in the presence of copper. These proteins are most likely involved in the formation and rearrangement of disulfide bonds in proteins in the periplasm. Copper ions catalyze the formation of incorrect disulfide bonds in proteins. However, the up-regulated disulfide isomerases found could restore native disufide bonds allowing cell survival. In conclusion, At. ferrooxidans may resist high copper concentrations by using additional copper resistance strategies in which cell envelope proteins are very important. This knowledge could be used to select the best fit members of the bioleaching community to attain more efficient industrial biomining processes.

You might also be interested in these eBooks

Integration of Scientific and Industrial Knowledge on Biohydrometallurgy

View Preview

Info:

Periodical:

Advanced Materials Research (Volume 825)

Pages:

206-209

DOI:

https://doi.org/10.4028/www.scientific.net/AMR.825.206

Citation:

Cite this paper

Online since:

October 2013

Authors:

Rodrigo Almarcegui, Claudio Navarro, Alberto Paradela, Diego von Bernath, Carlos A. Jerez*

Keywords:

At. ferrooxidans, Bioleaching, Copper Resistance, Disulfide Isomerase, Proteomics

Export:

RIS, BibTeX

Price:

Permissions CCC:

Request Permissions

Permissions PLS:

Request Permissions

Сopyright:

Citation:

* - Corresponding Author

References

[1] C.A. Jerez, The use of extremophilic microorganisms in the industrial recovery of metals. In extremophiles: Sustainable resources and Biotechnological Implications, in: Om. V. Singh (ed. ), John Wiley and sons, Inc., (2013), pp.319-334.

DOI: 10.1002/9781118394144.ch12

Google Scholar

[2] A. Orell, C.A. Navarro, R. Arancibia, J.C. Mobarec, C.A. Jerez, Life in blue: Copper resistance mechanisms of bacteria and Archaea used in industrial biomining of minerals, Biotechnol. Adv. 28 (2010) 839-848.

DOI: 10.1016/j.biotechadv.2010.07.003

Google Scholar

[3] M. Dopson, C. Baker-Austin, P.R. Koppineedi, L.B. Philip, Growth in sulfidic mineral enviroments: metal resistance mechanisms in acidophilic micro-organisms, Microbiol. 149 (2003) 1959-(1970).

DOI: 10.1099/mic.0.26296-0

Google Scholar

[4] C.A. Jerez, Bioleaching and biomining for the industrial recovery of metals. In: Murray Moo-Young (ed. ), Comprehensive Biotechnology, Second Edition, vol. 3, (2011), pp.717-729. Elsevier.

DOI: 10.1016/b978-0-08-088504-9.00234-8

Google Scholar

[5] D. Magnani, M. Solioz, How bacteria handle copper, Microbiol. Monogr. 6 (2007) 259-285.

Google Scholar

[6] C.A. Navarro, L.H. Orellana, C. Mauriaca, C.A. Jerez, Transcriptional and functional studies of Acidithiobacillus ferrooxidans genes related to survival in the presence of copper, Appl. Environ. Microbiol. 75 (2011) 6102-6109.

DOI: 10.1128/aem.00308-09

Google Scholar

[7] A. Chi, L. Valenzuela, S. Beard, A.J. Mackey, J. Shabanowitz, D.F. Hunt, C.A. Jerez, Periplasmic proteins of the extremophile Acidithiobacillus ferrooxidans: a high throughput proteomic analysis, Mol. Cell. Proteomics. 6 (2007) 2239-2251.

DOI: 10.1074/mcp.m700042-mcp200

Google Scholar

[8] S. Beard, A. Paradela, J.P. Albar, C.A. Jerez, Growth of Acidithiobacillus ferrooxidans ATCC 23270 in thiosulfate under oxygen-limiting conditions generate extracellular sulfur globules by means of a secreted tetrathionate hydrolase, Front. Microbio. 2: 79. doi: 10. 3389/fmicb. 2011. 00079.

DOI: 10.3389/fmicb.2011.00079

Google Scholar

[9] L.H. Orellana, C.A. Jerez, A genomic island provides Acidithiobacillus ferrooxidans ATCC 53993 additional copper resistance: a possible competitive advantage, Appl. Microbiol. Biotechnol. 92 (2011) 761-767.

DOI: 10.1007/s00253-011-3494-x

Google Scholar

[10] K. Ito, K. Inaba, The disulfide bond formation (Dsb) system, Curr. Opin. Struct. Biol. 18 (2008) 450-458.

DOI: 10.1016/j.sbi.2008.02.002

Google Scholar

[11] A. Hiniker, J.F. Collet, J. Bardwell, Copper stress causes an in vivo requirement for the Escherichia coli disulfide isomerase DsbC, J. Biol. Chem. 40 (2005) 33785-33791.

DOI: 10.1074/jbc.m505742200

Google Scholar