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N-Terminal Presequence-Independent Import of Phosphofructokinase into Hydrogenosomes of Trichomonas vaginalis
P. Rada, AR. Makki, V. Zimorski, S. Garg, V. Hampl, I. Hrdý, SB. Gould, J. Tachezy,
Jazyk angličtina Země Spojené státy americké
Typ dokumentu časopisecké články, práce podpořená grantem
NLK
Free Medical Journals
od 2002 do 2015
Freely Accessible Science Journals
od 2002 do 2015
PubMed Central
od 2002 do 2015
Europe PubMed Central
od 2002 do 2015
Open Access Digital Library
od 2002-02-01
PubMed
26475173
DOI
10.1128/ec.00104-15
Knihovny.cz E-zdroje
- MeSH
- adenosintrifosfát farmakologie MeSH
- difosfáty metabolismus MeSH
- ferredoxiny metabolismus MeSH
- fosfofruktokinasy chemie metabolismus MeSH
- fylogeneze MeSH
- mitochondrie účinky léků metabolismus MeSH
- molekulární sekvence - údaje MeSH
- organely účinky léků metabolismus MeSH
- promotorové oblasti (genetika) genetika MeSH
- Saccharomyces cerevisiae účinky léků metabolismus MeSH
- sekvence aminokyselin MeSH
- sekvenční seřazení MeSH
- transport proteinů účinky léků MeSH
- Trichomonas vaginalis účinky léků enzymologie MeSH
- vodík metabolismus MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
Mitochondrial evolution entailed the origin of protein import machinery that allows nuclear-encoded proteins to be targeted to the organelle, as well as the origin of cleavable N-terminal targeting sequences (NTS) that allow efficient sorting and import of matrix proteins. In hydrogenosomes and mitosomes, reduced forms of mitochondria with reduced proteomes, NTS-independent targeting of matrix proteins is known. Here, we studied the cellular localization of two glycolytic enzymes in the anaerobic pathogen Trichomonas vaginalis: PPi-dependent phosphofructokinase (TvPPi-PFK), which is the main glycolytic PFK activity of the protist, and ATP-dependent PFK (TvATP-PFK), the function of which is less clear. TvPPi-PFK was detected predominantly in the cytosol, as expected, while all four TvATP-PFK paralogues were imported into T. vaginalis hydrogenosomes, although none of them possesses an NTS. The heterologous expression of TvATP-PFK in Saccharomyces cerevisiae revealed an intrinsic capability of the protein to be recognized and imported into yeast mitochondria, whereas yeast ATP-PFK resides in the cytosol. TvATP-PFK consists of only a catalytic domain, similarly to "short" bacterial enzymes, while ScATP-PFK includes an N-terminal extension, a catalytic domain, and a C-terminal regulatory domain. Expression of the catalytic domain of ScATP-PFK and short Escherichia coli ATP-PFK in T. vaginalis resulted in their partial delivery to hydrogenosomes. These results indicate that TvATP-PFK and the homologous ATP-PFKs possess internal structural targeting information that is recognized by the hydrogenosomal import machinery. From an evolutionary perspective, the predisposition of ancient ATP-PFK to be recognized and imported into hydrogenosomes might be a relict from the early phases of organelle evolution.
Department of Parasitology Charles University Prague Faculty of Science Prague Czech Republic
Institute for Molecular Evolution Heinrich Heine University Düsseldorf Düsseldorf Germany
Citace poskytuje Crossref.org
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