Author | dc.contributor.author | Chi, An | |
Author | dc.contributor.author | Valenzuela, Lissette | es_CL |
Author | dc.contributor.author | Beard, Simon | es_CL |
Author | dc.contributor.author | Mackey, Aaron J. | es_CL |
Author | dc.contributor.author | Shabanowitz, Jeffrey | es_CL |
Author | dc.contributor.author | Hunt, Donald F. | es_CL |
Author | dc.contributor.author | Jerez Guevara, Carlos | es_CL |
Admission date | dc.date.accessioned | 2011-03-31T12:00:01Z | |
Available date | dc.date.available | 2011-03-31T12:00:01Z | |
Publication date | dc.date.issued | 2007-10-02 | |
Cita de ítem | dc.identifier.citation | MOLECULAR & CELLULAR PROTEOMICS, Volume: 6, Issue: 12, Pages: 2239-2251, 2007 | en_US |
Identifier | dc.identifier.issn | 1535-9476 | |
Identifier | dc.identifier.uri | https://repositorio.uchile.cl/handle/2250/119127 | |
Abstract | dc.description.abstract | Acidithiobacillus 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 |
Patrocinador | dc.description.sponsorship | This 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 |
Lenguage | dc.language.iso | en | en_US |
Publisher | dc.publisher | AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC | en_US |
Keywords | dc.subject | BACTERIAL OUTER-MEMBRANE | en_US |
Título | dc.title | Periplasmic proteins of the extremophile Acidithiobacillus ferrooxidans | en_US |
Document type | dc.type | Artículo de revista | |