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Nitrogen starvation induces extensive changes in the redox proteome of Prochlorococcus sp. strain SS120
Author(s) -
McDonagh Brian,
DomínguezMartín Ma Agustina,
GómezBaena Guadalupe,
LópezLozano Antonio,
Diez Jesús,
Bárcena Jose A.,
García Fernández Jose M.
Publication year - 2012
Publication title -
environmental microbiology reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.229
H-Index - 69
ISSN - 1758-2229
DOI - 10.1111/j.1758-2229.2012.00329.x
Subject(s) - prochlorococcus , proteome , biochemistry , glutamine synthetase , redox , biology , metabolic pathway , metabolism , isocitrate dehydrogenase , chemistry , enzyme , cyanobacteria , glutamine , bacteria , amino acid , synechococcus , genetics , organic chemistry
Summary Very low nitrogen concentration is a critical limitation in the oligotrophic oceans inhabited by the cyanobacterium Prochlorococccus , one of the main primary producers on Earth. It is well known that nitrogen starvation affects redox homeostasis in cells. We have studied the effect of nitrogen starvation on the thiol redox proteome in the Prochlorococcus sp. SS120 strain, by using shotgun proteomic techniques to map the cysteine modified in each case and to quantify the ratio of reversibly oxidized/reduced species. We identified a number of proteins showing modified cysteines only under either control or N‐starvation, including isocitrate dehydrogenase and ribulose phosphate 3‐epimerase. We detected other key enzymes, such as glutamine synthetase, transporters and transaminases, showing that nitrogen‐related pathways were deeply affected by nitrogen starvation. Reversibly oxidized cysteines were also detected in proteins of other important metabolic pathways, such as photosynthesis, phosphorus metabolism, ATP synthesis and nucleic acids metabolism. Our results demonstrate a wide effect of nitrogen limitation on the redox status of the Prochlorococcus proteome, suggesting that besides previously reported transcriptional changes, this cyanobacterium responds with post‐translational redox changes to the lack of nitrogen in its environment.