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Authordc.contributor.authorChi, An 
Authordc.contributor.authorValenzuela, Lissette es_CL
Authordc.contributor.authorBeard, Simon es_CL
Authordc.contributor.authorMackey, Aaron J. es_CL
Authordc.contributor.authorShabanowitz, Jeffrey es_CL
Authordc.contributor.authorHunt, Donald F. es_CL
Authordc.contributor.authorJerez Guevara, Carlos es_CL
Admission datedc.date.accessioned2011-03-31T12:00:01Z
Available datedc.date.available2011-03-31T12:00:01Z
Publication datedc.date.issued2007-10-02
Cita de ítemdc.identifier.citationMOLECULAR & CELLULAR PROTEOMICS, Volume: 6, Issue: 12, Pages: 2239-2251, 2007en_US
Identifierdc.identifier.issn1535-9476
Identifierdc.identifier.urihttps://repositorio.uchile.cl/handle/2250/119127
Abstractdc.description.abstractAcidithiobacillus ferrooxidans is a chemolithoautotrophic acidophile capable of obtaining energy by oxidizing ferrous iron or sulfur compounds such as metal sulfides. Some of the proteins involved in these oxidations have been described as forming part of the periplasm of this extremophile. The detailed study of the periplasmic components constitutes an important area to understand the physiology and environmental interactions of microorganisms. Proteomics analysis of the periplasmic fraction of A. ferrooxidans ATCC 23270 was performed by using high resolution linear ion trap-FT MS. We identified a total of 131 proteins in the periplasm of the microorganism grown in thiosulfate. When possible, functional categories were assigned to the proteins: 13.8% were transport and binding proteins, 14.6% were several kinds of cell envelope proteins, 10.8% were involved in energy metabolism, 10% were related to protein fate and folding, 10% were proteins with unknown functions, and 26.1% were proteins without homologues in databases. These last proteins are most likely characteristic of A. ferrooxidans and may have important roles yet to be assigned. The majority of the periplasmic proteins from A. ferrooxidans were very basic compared with those of neutrophilic microorganisms such as Escherichia coli, suggesting a special adaptation of the chemolithoautotrophic bacterium to its very acidic environment. The high throughput proteomics approach used here not only helps to understand the physiology of this extreme acidophile but also offers an important contribution to the functional annotation for the available genomes of biomining microorganisms such as A. ferrooxidans for which no efficient genetic systems are available to disrupt genes by procedures such as homologous recombination.en_US
Patrocinadordc.description.sponsorshipThis work was supported in part by Project Fondo de Ciencia y Tecnología 1030767, by Iniciativa Científica Milenio Project P-05- 001-F, and by National Institutes of Health Grant GM37537 (to D. F. H.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked “advertisement” in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.en_US
Lenguagedc.language.isoenen_US
Publisherdc.publisherAMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INCen_US
Keywordsdc.subjectBACTERIAL OUTER-MEMBRANEen_US
Títulodc.titlePeriplasmic proteins of the extremophile Acidithiobacillus ferrooxidansen_US
Document typedc.typeArtículo de revista


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