Iron-induced changes in the proteome of Trichomonas vaginalis hydrogenosomes
Jazyk angličtina Země Spojené státy americké Médium electronic-print
Typ dokumentu časopisecké články, práce podpořená grantem
PubMed
23741475
PubMed Central
PMC3669245
DOI
10.1371/journal.pone.0065148
PII: PONE-D-13-09591
Knihovny.cz E-zdroje
- MeSH
- energetický metabolismus MeSH
- hmotnostní spektrometrie MeSH
- lidé MeSH
- organely metabolismus ultrastruktura MeSH
- oxidace-redukce MeSH
- proteom metabolismus MeSH
- proteomika MeSH
- protozoální proteiny chemie metabolismus MeSH
- regulace genové exprese MeSH
- shluková analýza MeSH
- síra metabolismus MeSH
- Trichomonas vaginalis genetika metabolismus MeSH
- železo metabolismus MeSH
- Check Tag
- lidé MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- proteom MeSH
- protozoální proteiny MeSH
- síra MeSH
- železo MeSH
Iron plays a crucial role in metabolism as a key component of catalytic and redox cofactors, such as heme or iron-sulfur clusters in enzymes and electron-transporting or regulatory proteins. Limitation of iron availability by the host is also one of the mechanisms involved in immunity. Pathogens must regulate their protein expression according to the iron concentration in their environment and optimize their metabolic pathways in cases of limitation through the availability of respective cofactors. Trichomonas vaginalis, a sexually transmitted pathogen of humans, requires high iron levels for optimal growth. It is an anaerobe that possesses hydrogenosomes, mitochondrion-related organelles that harbor pathways of energy metabolism and iron-sulfur cluster assembly. We analyzed the proteomes of hydrogenosomes obtained from cells cultivated under iron-rich and iron-deficient conditions employing two-dimensional peptide separation combining IEF and nano-HPLC with quantitative MALDI-MS/MS. We identified 179 proteins, of which 58 were differentially expressed. Iron deficiency led to the upregulation of proteins involved in iron-sulfur cluster assembly and the downregulation of enzymes involved in carbohydrate metabolism. Interestingly, iron affected the expression of only some of multiple protein paralogues, whereas the expression of others was iron independent. This finding indicates a stringent regulation of differentially expressed multiple gene copies in response to changes in the availability of exogenous iron.
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