title: Response to copper of Acidithiobacillus ferrooxidans ATCC 23270 grown in elemental sulfur.
abstract: The response of Acidithiobacillus ferrooxidans ATCC 23270 to copper was analyzed in sulfur-grown cells by using quantitative proteomics. Forty-seven proteins showed altered levels in cells grown in the presence of 50 mM copper sulfate. Of these proteins, 24 were up-regulated and 23 down-regulated. As seen before in ferrous iron-grown cells, there was a notorious up-regulation of RND-type Cus systems and different RND-type efflux pumps, indicating that these proteins are very important in copper resistance. Copper also triggered the down-regulation of the major outer membrane porin of A. ferrooxidans in sulfur-grown bacteria, suggesting they respond to the metal by decreasing the influx of cations into the cell. On the contrary, copper in sulfur-grown cells caused an overexpression of putative TadA and TadB proteins known to be essential for biofilm formation in bacteria. Surprisingly, sulfur-grown microorganisms showed increased levels of proteins related with energy generation (rus and petII operons) in the presence of copper. Although rus operon is overexpressed mainly in cells grown in ferrous iron, the up-regulation of rusticyanin in sulfur indicates a possible role for this protein in copper resistance as well. Finally, copper response in A. ferrooxidans appears to be influenced by the substrate being oxidized by the microorganism.
authors.affiliation: Laboratory of Molecular Microbiology and Biotechnology, Department of Biology, Faculty of Sciences, University of Chile, Santiago, Chile. Electronic address: almarcegui@live.cl.
authors.forename: Rodrigo J
authors.initials: RJ
authors.lastname: Almárcegui
authors.affiliation: Laboratory of Molecular Microbiology and Biotechnology, Department of Biology, Faculty of Sciences, University of Chile, Santiago, Chile. Electronic address: clnavarrol@gmail.com.
authors.forename: Claudio A
authors.initials: CA
authors.lastname: Navarro
authors.affiliation: Proteomics Laboratory, National Biotechnology Center, Madrid, Spain. Electronic address: Alberto.paradela@cnb.csic.es.
authors.forename: Alberto
authors.initials: A
authors.lastname: Paradela
authors.affiliation: Proteomics Laboratory, National Biotechnology Center, Madrid, Spain. Electronic address: jpalbar@cnb.csic.es.
authors.forename: Juan Pablo
authors.initials: JP
authors.lastname: Albar
authors.affiliation: Laboratory of Molecular Microbiology and Biotechnology, Department of Biology, Faculty of Sciences, University of Chile, Santiago, Chile. Electronic address: dvonbernath@gmail.com.
authors.forename: Diego
authors.initials: D
authors.lastname: von Bernath
authors.affiliation: Laboratory of Molecular Microbiology and Biotechnology, Department of Biology, Faculty of Sciences, University of Chile, Santiago, Chile. Electronic address: cjerez@uchile.cl.
authors.forename: Carlos A
authors.initials: CA
authors.lastname: Jerez
mesh_terms: D042763:Acidithiobacillus / Q000737:chemistry* / Q000187:drug effects* / Q000254:growth & development / Q000378:metabolism; D001426:Bacterial Proteins / Q000032:analysis*; D003300:Copper / Q000378:metabolism*; D020869:Gene Expression Profiling; D020543:Proteome / Q000032:analysis*; D013312:Stress, Physiological; D013455:Sulfur / Q000378:metabolism*
chemical_list: D001426:Bacterial Proteins; D020543:Proteome; D013455:Sulfur; D003300:Copper
keywords: Acidophile; Biomining; Copper resistance; Proteomics